data_9MTV
# 
_entry.id   9MTV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MTV         pdb_00009mtv 10.2210/pdb9mtv/pdb 
WWPDB D_1000291829 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-23 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.page_first'              
6  2 'Structure model' '_citation.page_last'               
7  2 'Structure model' '_citation.pdbx_database_id_DOI'    
8  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
9  2 'Structure model' '_citation.title'                   
10 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MTV 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9MTU 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              csmith@slac.stanford.edu 
_pdbx_contact_author.name_first         Clyde 
_pdbx_contact_author.name_last          Smith 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1885-1511 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smith, C.A.'     1 ? 
'Stewart, N.K.'   2 ? 
'Vakulenko, S.B.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Mbio 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2150-7511 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                e0018525 
_citation.page_last                 e0018525 
_citation.title                     'Evolution of carbapenemase activity in the class C beta-lactamase ADC-1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/mbio.00185-25 
_citation.pdbx_database_id_PubMed   40293226 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Stewart, N.K.'    1 0009-0008-2856-420X 
primary 'Toth, M.'         2 ?                   
primary 'Bhattacharya, M.' 3 ?                   
primary 'Smith, C.A.'      4 0000-0002-1885-1511 
primary 'Vakulenko, S.B.'  5 0000-0002-5327-8124 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Beta-lactamase 40596.277 2   3.5.2.6 'V294F, S317T, F321S' ? 'triple mutant ADC-1 beta-lactamase' 
2 non-polymer syn 'NITRATE ION'  62.005    1   ?       ?                     ? ?                                    
3 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?       ?                     ? ?                                    
4 water       nat water          18.015    305 ?       ?                     ? ?                                    
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIFMKPNKVTAISKEPSVKMYHKTGTTNRS
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIFMKPNKVTAISKEPSVKMYHKTGTTNRS
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NITRATE ION'  NO3 
3 1,2-ETHANEDIOL EDO 
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASN n 
1 3   THR n 
1 4   PRO n 
1 5   LYS n 
1 6   ASP n 
1 7   GLN n 
1 8   GLU n 
1 9   ILE n 
1 10  LYS n 
1 11  LYS n 
1 12  LEU n 
1 13  VAL n 
1 14  ASP n 
1 15  GLN n 
1 16  ASN n 
1 17  PHE n 
1 18  LYS n 
1 19  PRO n 
1 20  LEU n 
1 21  LEU n 
1 22  GLU n 
1 23  LYS n 
1 24  TYR n 
1 25  ASP n 
1 26  VAL n 
1 27  PRO n 
1 28  GLY n 
1 29  MET n 
1 30  ALA n 
1 31  VAL n 
1 32  GLY n 
1 33  VAL n 
1 34  ILE n 
1 35  GLN n 
1 36  ASN n 
1 37  ASN n 
1 38  LYS n 
1 39  LYS n 
1 40  TYR n 
1 41  GLU n 
1 42  MET n 
1 43  TYR n 
1 44  TYR n 
1 45  GLY n 
1 46  LEU n 
1 47  GLN n 
1 48  SER n 
1 49  VAL n 
1 50  GLN n 
1 51  ASP n 
1 52  LYS n 
1 53  LYS n 
1 54  ALA n 
1 55  VAL n 
1 56  ASN n 
1 57  SER n 
1 58  SER n 
1 59  THR n 
1 60  ILE n 
1 61  PHE n 
1 62  GLU n 
1 63  LEU n 
1 64  GLY n 
1 65  SER n 
1 66  VAL n 
1 67  SER n 
1 68  LYS n 
1 69  LEU n 
1 70  PHE n 
1 71  THR n 
1 72  ALA n 
1 73  THR n 
1 74  ALA n 
1 75  GLY n 
1 76  GLY n 
1 77  TYR n 
1 78  ALA n 
1 79  LYS n 
1 80  ASN n 
1 81  LYS n 
1 82  GLY n 
1 83  LYS n 
1 84  ILE n 
1 85  SER n 
1 86  PHE n 
1 87  ASP n 
1 88  ASP n 
1 89  THR n 
1 90  PRO n 
1 91  GLY n 
1 92  LYS n 
1 93  TYR n 
1 94  TRP n 
1 95  LYS n 
1 96  GLU n 
1 97  LEU n 
1 98  LYS n 
1 99  ASN n 
1 100 THR n 
1 101 PRO n 
1 102 ILE n 
1 103 ASP n 
1 104 GLN n 
1 105 VAL n 
1 106 ASN n 
1 107 LEU n 
1 108 LEU n 
1 109 GLN n 
1 110 LEU n 
1 111 ALA n 
1 112 THR n 
1 113 TYR n 
1 114 THR n 
1 115 SER n 
1 116 GLY n 
1 117 ASN n 
1 118 LEU n 
1 119 ALA n 
1 120 LEU n 
1 121 GLN n 
1 122 PHE n 
1 123 PRO n 
1 124 ASP n 
1 125 GLU n 
1 126 VAL n 
1 127 LYS n 
1 128 THR n 
1 129 ASP n 
1 130 GLN n 
1 131 GLN n 
1 132 VAL n 
1 133 LEU n 
1 134 THR n 
1 135 PHE n 
1 136 PHE n 
1 137 LYS n 
1 138 ASP n 
1 139 TRP n 
1 140 LYS n 
1 141 PRO n 
1 142 LYS n 
1 143 ASN n 
1 144 SER n 
1 145 ILE n 
1 146 GLY n 
1 147 GLU n 
1 148 TYR n 
1 149 ARG n 
1 150 GLN n 
1 151 TYR n 
1 152 SER n 
1 153 ASN n 
1 154 PRO n 
1 155 SER n 
1 156 ILE n 
1 157 GLY n 
1 158 LEU n 
1 159 PHE n 
1 160 GLY n 
1 161 LYS n 
1 162 VAL n 
1 163 VAL n 
1 164 ALA n 
1 165 LEU n 
1 166 SER n 
1 167 MET n 
1 168 ASN n 
1 169 LYS n 
1 170 PRO n 
1 171 PHE n 
1 172 ASP n 
1 173 GLN n 
1 174 VAL n 
1 175 LEU n 
1 176 GLU n 
1 177 LYS n 
1 178 THR n 
1 179 ILE n 
1 180 PHE n 
1 181 PRO n 
1 182 ALA n 
1 183 LEU n 
1 184 GLY n 
1 185 LEU n 
1 186 LYS n 
1 187 HIS n 
1 188 SER n 
1 189 TYR n 
1 190 VAL n 
1 191 ASN n 
1 192 VAL n 
1 193 PRO n 
1 194 LYS n 
1 195 THR n 
1 196 GLN n 
1 197 MET n 
1 198 GLN n 
1 199 ASN n 
1 200 TYR n 
1 201 ALA n 
1 202 PHE n 
1 203 GLY n 
1 204 TYR n 
1 205 ASN n 
1 206 GLN n 
1 207 GLU n 
1 208 ASN n 
1 209 GLN n 
1 210 PRO n 
1 211 ILE n 
1 212 ARG n 
1 213 VAL n 
1 214 ASN n 
1 215 PRO n 
1 216 GLY n 
1 217 PRO n 
1 218 LEU n 
1 219 GLY n 
1 220 ALA n 
1 221 PRO n 
1 222 ALA n 
1 223 TYR n 
1 224 GLY n 
1 225 VAL n 
1 226 LYS n 
1 227 SER n 
1 228 THR n 
1 229 LEU n 
1 230 PRO n 
1 231 ASP n 
1 232 MET n 
1 233 LEU n 
1 234 SER n 
1 235 PHE n 
1 236 ILE n 
1 237 HIS n 
1 238 ALA n 
1 239 ASN n 
1 240 LEU n 
1 241 ASN n 
1 242 PRO n 
1 243 GLN n 
1 244 LYS n 
1 245 TYR n 
1 246 PRO n 
1 247 ALA n 
1 248 ASP n 
1 249 ILE n 
1 250 GLN n 
1 251 ARG n 
1 252 ALA n 
1 253 ILE n 
1 254 ASN n 
1 255 GLU n 
1 256 THR n 
1 257 HIS n 
1 258 GLN n 
1 259 GLY n 
1 260 ARG n 
1 261 TYR n 
1 262 GLN n 
1 263 VAL n 
1 264 ASN n 
1 265 THR n 
1 266 MET n 
1 267 TYR n 
1 268 GLN n 
1 269 ALA n 
1 270 LEU n 
1 271 GLY n 
1 272 TRP n 
1 273 GLU n 
1 274 GLU n 
1 275 PHE n 
1 276 SER n 
1 277 TYR n 
1 278 PRO n 
1 279 ALA n 
1 280 THR n 
1 281 LEU n 
1 282 GLN n 
1 283 THR n 
1 284 LEU n 
1 285 LEU n 
1 286 ASP n 
1 287 SER n 
1 288 ASN n 
1 289 SER n 
1 290 GLU n 
1 291 GLN n 
1 292 ILE n 
1 293 PHE n 
1 294 MET n 
1 295 LYS n 
1 296 PRO n 
1 297 ASN n 
1 298 LYS n 
1 299 VAL n 
1 300 THR n 
1 301 ALA n 
1 302 ILE n 
1 303 SER n 
1 304 LYS n 
1 305 GLU n 
1 306 PRO n 
1 307 SER n 
1 308 VAL n 
1 309 LYS n 
1 310 MET n 
1 311 TYR n 
1 312 HIS n 
1 313 LYS n 
1 314 THR n 
1 315 GLY n 
1 316 THR n 
1 317 THR n 
1 318 ASN n 
1 319 ARG n 
1 320 SER n 
1 321 GLY n 
1 322 THR n 
1 323 TYR n 
1 324 VAL n 
1 325 VAL n 
1 326 PHE n 
1 327 ILE n 
1 328 PRO n 
1 329 LYS n 
1 330 GLU n 
1 331 ASN n 
1 332 ILE n 
1 333 GLY n 
1 334 LEU n 
1 335 VAL n 
1 336 MET n 
1 337 LEU n 
1 338 THR n 
1 339 ASN n 
1 340 LYS n 
1 341 ARG n 
1 342 ILE n 
1 343 PRO n 
1 344 ASN n 
1 345 GLU n 
1 346 GLU n 
1 347 ARG n 
1 348 ILE n 
1 349 LYS n 
1 350 ALA n 
1 351 ALA n 
1 352 TYR n 
1 353 ALA n 
1 354 VAL n 
1 355 LEU n 
1 356 ASN n 
1 357 ALA n 
1 358 ILE n 
1 359 LYS n 
1 360 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   360 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ampC 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
NO3 non-polymer         . 'NITRATE ION'   ?                 'N O3 -1'        62.005  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   ASN 2   3   3   ASN ASN A . n 
A 1 3   THR 3   4   4   THR THR A . n 
A 1 4   PRO 4   5   5   PRO PRO A . n 
A 1 5   LYS 5   6   6   LYS LYS A . n 
A 1 6   ASP 6   7   7   ASP ASP A . n 
A 1 7   GLN 7   8   8   GLN GLN A . n 
A 1 8   GLU 8   9   9   GLU GLU A . n 
A 1 9   ILE 9   10  10  ILE ILE A . n 
A 1 10  LYS 10  11  11  LYS LYS A . n 
A 1 11  LYS 11  12  12  LYS LYS A . n 
A 1 12  LEU 12  13  13  LEU LEU A . n 
A 1 13  VAL 13  14  14  VAL VAL A . n 
A 1 14  ASP 14  15  15  ASP ASP A . n 
A 1 15  GLN 15  16  16  GLN GLN A . n 
A 1 16  ASN 16  17  17  ASN ASN A . n 
A 1 17  PHE 17  18  18  PHE PHE A . n 
A 1 18  LYS 18  19  19  LYS LYS A . n 
A 1 19  PRO 19  20  20  PRO PRO A . n 
A 1 20  LEU 20  21  21  LEU LEU A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  GLU 22  23  23  GLU GLU A . n 
A 1 23  LYS 23  24  24  LYS LYS A . n 
A 1 24  TYR 24  25  25  TYR TYR A . n 
A 1 25  ASP 25  26  26  ASP ASP A . n 
A 1 26  VAL 26  27  27  VAL VAL A . n 
A 1 27  PRO 27  28  28  PRO PRO A . n 
A 1 28  GLY 28  29  29  GLY GLY A . n 
A 1 29  MET 29  30  30  MET MET A . n 
A 1 30  ALA 30  31  31  ALA ALA A . n 
A 1 31  VAL 31  32  32  VAL VAL A . n 
A 1 32  GLY 32  33  33  GLY GLY A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  ILE 34  35  35  ILE ILE A . n 
A 1 35  GLN 35  36  36  GLN GLN A . n 
A 1 36  ASN 36  37  37  ASN ASN A . n 
A 1 37  ASN 37  38  38  ASN ASN A . n 
A 1 38  LYS 38  39  39  LYS LYS A . n 
A 1 39  LYS 39  40  40  LYS LYS A . n 
A 1 40  TYR 40  41  41  TYR TYR A . n 
A 1 41  GLU 41  42  42  GLU GLU A . n 
A 1 42  MET 42  43  43  MET MET A . n 
A 1 43  TYR 43  44  44  TYR TYR A . n 
A 1 44  TYR 44  45  45  TYR TYR A . n 
A 1 45  GLY 45  46  46  GLY GLY A . n 
A 1 46  LEU 46  47  47  LEU LEU A . n 
A 1 47  GLN 47  48  48  GLN GLN A . n 
A 1 48  SER 48  49  49  SER SER A . n 
A 1 49  VAL 49  50  50  VAL VAL A . n 
A 1 50  GLN 50  51  51  GLN GLN A . n 
A 1 51  ASP 51  52  52  ASP ASP A . n 
A 1 52  LYS 52  53  53  LYS LYS A . n 
A 1 53  LYS 53  54  54  LYS LYS A . n 
A 1 54  ALA 54  55  55  ALA ALA A . n 
A 1 55  VAL 55  56  56  VAL VAL A . n 
A 1 56  ASN 56  57  57  ASN ASN A . n 
A 1 57  SER 57  58  58  SER SER A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  THR 59  60  60  THR THR A . n 
A 1 60  ILE 60  61  61  ILE ILE A . n 
A 1 61  PHE 61  62  62  PHE PHE A . n 
A 1 62  GLU 62  63  63  GLU GLU A . n 
A 1 63  LEU 63  64  64  LEU LEU A . n 
A 1 64  GLY 64  65  65  GLY GLY A . n 
A 1 65  SER 65  66  66  SER SER A . n 
A 1 66  VAL 66  67  67  VAL VAL A . n 
A 1 67  SER 67  68  68  SER SER A . n 
A 1 68  LYS 68  69  69  LYS LYS A . n 
A 1 69  LEU 69  70  70  LEU LEU A . n 
A 1 70  PHE 70  71  71  PHE PHE A . n 
A 1 71  THR 71  72  72  THR THR A . n 
A 1 72  ALA 72  73  73  ALA ALA A . n 
A 1 73  THR 73  74  74  THR THR A . n 
A 1 74  ALA 74  75  75  ALA ALA A . n 
A 1 75  GLY 75  76  76  GLY GLY A . n 
A 1 76  GLY 76  77  77  GLY GLY A . n 
A 1 77  TYR 77  78  78  TYR TYR A . n 
A 1 78  ALA 78  79  79  ALA ALA A . n 
A 1 79  LYS 79  80  80  LYS LYS A . n 
A 1 80  ASN 80  81  81  ASN ASN A . n 
A 1 81  LYS 81  82  82  LYS LYS A . n 
A 1 82  GLY 82  83  83  GLY GLY A . n 
A 1 83  LYS 83  84  84  LYS LYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  SER 85  86  86  SER SER A . n 
A 1 86  PHE 86  87  87  PHE PHE A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  ASP 88  89  89  ASP ASP A . n 
A 1 89  THR 89  90  90  THR THR A . n 
A 1 90  PRO 90  91  91  PRO PRO A . n 
A 1 91  GLY 91  92  92  GLY GLY A . n 
A 1 92  LYS 92  93  93  LYS LYS A . n 
A 1 93  TYR 93  94  94  TYR TYR A . n 
A 1 94  TRP 94  95  95  TRP TRP A . n 
A 1 95  LYS 95  96  96  LYS LYS A . n 
A 1 96  GLU 96  97  97  GLU GLU A . n 
A 1 97  LEU 97  98  98  LEU LEU A . n 
A 1 98  LYS 98  99  99  LYS LYS A . n 
A 1 99  ASN 99  100 100 ASN ASN A . n 
A 1 100 THR 100 101 101 THR THR A . n 
A 1 101 PRO 101 102 102 PRO PRO A . n 
A 1 102 ILE 102 103 103 ILE ILE A . n 
A 1 103 ASP 103 104 104 ASP ASP A . n 
A 1 104 GLN 104 105 105 GLN GLN A . n 
A 1 105 VAL 105 106 106 VAL VAL A . n 
A 1 106 ASN 106 107 107 ASN ASN A . n 
A 1 107 LEU 107 108 108 LEU LEU A . n 
A 1 108 LEU 108 109 109 LEU LEU A . n 
A 1 109 GLN 109 110 110 GLN GLN A . n 
A 1 110 LEU 110 111 111 LEU LEU A . n 
A 1 111 ALA 111 112 112 ALA ALA A . n 
A 1 112 THR 112 113 113 THR THR A . n 
A 1 113 TYR 113 114 114 TYR TYR A . n 
A 1 114 THR 114 115 115 THR THR A . n 
A 1 115 SER 115 116 116 SER SER A . n 
A 1 116 GLY 116 117 117 GLY GLY A . n 
A 1 117 ASN 117 118 118 ASN ASN A . n 
A 1 118 LEU 118 119 119 LEU LEU A . n 
A 1 119 ALA 119 120 120 ALA ALA A . n 
A 1 120 LEU 120 121 121 LEU LEU A . n 
A 1 121 GLN 121 122 122 GLN GLN A . n 
A 1 122 PHE 122 123 123 PHE PHE A . n 
A 1 123 PRO 123 124 124 PRO PRO A . n 
A 1 124 ASP 124 125 125 ASP ASP A . n 
A 1 125 GLU 125 126 126 GLU GLU A . n 
A 1 126 VAL 126 127 127 VAL VAL A . n 
A 1 127 LYS 127 128 128 LYS LYS A . n 
A 1 128 THR 128 129 129 THR THR A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 GLN 130 131 131 GLN GLN A . n 
A 1 131 GLN 131 132 132 GLN GLN A . n 
A 1 132 VAL 132 133 133 VAL VAL A . n 
A 1 133 LEU 133 134 134 LEU LEU A . n 
A 1 134 THR 134 135 135 THR THR A . n 
A 1 135 PHE 135 136 136 PHE PHE A . n 
A 1 136 PHE 136 137 137 PHE PHE A . n 
A 1 137 LYS 137 138 138 LYS LYS A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 TRP 139 140 140 TRP TRP A . n 
A 1 140 LYS 140 141 141 LYS LYS A . n 
A 1 141 PRO 141 142 142 PRO PRO A . n 
A 1 142 LYS 142 143 143 LYS LYS A . n 
A 1 143 ASN 143 144 144 ASN ASN A . n 
A 1 144 SER 144 145 145 SER SER A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 GLY 146 147 147 GLY GLY A . n 
A 1 147 GLU 147 148 148 GLU GLU A . n 
A 1 148 TYR 148 149 149 TYR TYR A . n 
A 1 149 ARG 149 150 150 ARG ARG A . n 
A 1 150 GLN 150 151 151 GLN GLN A . n 
A 1 151 TYR 151 152 152 TYR TYR A . n 
A 1 152 SER 152 153 153 SER SER A . n 
A 1 153 ASN 153 154 154 ASN ASN A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 SER 155 156 156 SER SER A . n 
A 1 156 ILE 156 157 157 ILE ILE A . n 
A 1 157 GLY 157 158 158 GLY GLY A . n 
A 1 158 LEU 158 159 159 LEU LEU A . n 
A 1 159 PHE 159 160 160 PHE PHE A . n 
A 1 160 GLY 160 161 161 GLY GLY A . n 
A 1 161 LYS 161 162 162 LYS LYS A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 VAL 163 164 164 VAL VAL A . n 
A 1 164 ALA 164 165 165 ALA ALA A . n 
A 1 165 LEU 165 166 166 LEU LEU A . n 
A 1 166 SER 166 167 167 SER SER A . n 
A 1 167 MET 167 168 168 MET MET A . n 
A 1 168 ASN 168 169 169 ASN ASN A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 PRO 170 171 171 PRO PRO A . n 
A 1 171 PHE 171 172 172 PHE PHE A . n 
A 1 172 ASP 172 173 173 ASP ASP A . n 
A 1 173 GLN 173 174 174 GLN GLN A . n 
A 1 174 VAL 174 175 175 VAL VAL A . n 
A 1 175 LEU 175 176 176 LEU LEU A . n 
A 1 176 GLU 176 177 177 GLU GLU A . n 
A 1 177 LYS 177 178 178 LYS LYS A . n 
A 1 178 THR 178 179 179 THR THR A . n 
A 1 179 ILE 179 180 180 ILE ILE A . n 
A 1 180 PHE 180 181 181 PHE PHE A . n 
A 1 181 PRO 181 182 182 PRO PRO A . n 
A 1 182 ALA 182 183 183 ALA ALA A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 GLY 184 185 185 GLY GLY A . n 
A 1 185 LEU 185 186 186 LEU LEU A . n 
A 1 186 LYS 186 187 187 LYS LYS A . n 
A 1 187 HIS 187 188 188 HIS HIS A . n 
A 1 188 SER 188 189 189 SER SER A . n 
A 1 189 TYR 189 190 190 TYR TYR A . n 
A 1 190 VAL 190 191 191 VAL VAL A . n 
A 1 191 ASN 191 192 192 ASN ASN A . n 
A 1 192 VAL 192 193 193 VAL VAL A . n 
A 1 193 PRO 193 194 194 PRO PRO A . n 
A 1 194 LYS 194 195 195 LYS LYS A . n 
A 1 195 THR 195 196 196 THR THR A . n 
A 1 196 GLN 196 197 197 GLN GLN A . n 
A 1 197 MET 197 198 198 MET MET A . n 
A 1 198 GLN 198 199 199 GLN GLN A . n 
A 1 199 ASN 199 200 200 ASN ASN A . n 
A 1 200 TYR 200 201 201 TYR TYR A . n 
A 1 201 ALA 201 202 202 ALA ALA A . n 
A 1 202 PHE 202 203 203 PHE PHE A . n 
A 1 203 GLY 203 204 204 GLY GLY A . n 
A 1 204 TYR 204 205 205 TYR TYR A . n 
A 1 205 ASN 205 206 206 ASN ASN A . n 
A 1 206 GLN 206 207 207 GLN GLN A . n 
A 1 207 GLU 207 208 208 GLU GLU A . n 
A 1 208 ASN 208 209 209 ASN ASN A . n 
A 1 209 GLN 209 210 210 GLN GLN A . n 
A 1 210 PRO 210 211 211 PRO PRO A . n 
A 1 211 ILE 211 212 212 ILE ILE A . n 
A 1 212 ARG 212 213 213 ARG ARG A . n 
A 1 213 VAL 213 214 214 VAL VAL A . n 
A 1 214 ASN 214 215 215 ASN ASN A . n 
A 1 215 PRO 215 216 216 PRO PRO A . n 
A 1 216 GLY 216 217 217 GLY GLY A . n 
A 1 217 PRO 217 218 218 PRO PRO A . n 
A 1 218 LEU 218 219 219 LEU LEU A . n 
A 1 219 GLY 219 220 220 GLY GLY A . n 
A 1 220 ALA 220 221 221 ALA ALA A . n 
A 1 221 PRO 221 222 222 PRO PRO A . n 
A 1 222 ALA 222 223 223 ALA ALA A . n 
A 1 223 TYR 223 224 224 TYR TYR A . n 
A 1 224 GLY 224 225 225 GLY GLY A . n 
A 1 225 VAL 225 226 226 VAL VAL A . n 
A 1 226 LYS 226 227 227 LYS LYS A . n 
A 1 227 SER 227 228 228 SER SER A . n 
A 1 228 THR 228 229 229 THR THR A . n 
A 1 229 LEU 229 230 230 LEU LEU A . n 
A 1 230 PRO 230 231 231 PRO PRO A . n 
A 1 231 ASP 231 232 232 ASP ASP A . n 
A 1 232 MET 232 233 233 MET MET A . n 
A 1 233 LEU 233 234 234 LEU LEU A . n 
A 1 234 SER 234 235 235 SER SER A . n 
A 1 235 PHE 235 236 236 PHE PHE A . n 
A 1 236 ILE 236 237 237 ILE ILE A . n 
A 1 237 HIS 237 238 238 HIS HIS A . n 
A 1 238 ALA 238 239 239 ALA ALA A . n 
A 1 239 ASN 239 240 240 ASN ASN A . n 
A 1 240 LEU 240 241 241 LEU LEU A . n 
A 1 241 ASN 241 242 242 ASN ASN A . n 
A 1 242 PRO 242 243 243 PRO PRO A . n 
A 1 243 GLN 243 244 244 GLN GLN A . n 
A 1 244 LYS 244 245 245 LYS LYS A . n 
A 1 245 TYR 245 246 246 TYR TYR A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 ASP 248 249 249 ASP ASP A . n 
A 1 249 ILE 249 250 250 ILE ILE A . n 
A 1 250 GLN 250 251 251 GLN GLN A . n 
A 1 251 ARG 251 252 252 ARG ARG A . n 
A 1 252 ALA 252 253 253 ALA ALA A . n 
A 1 253 ILE 253 254 254 ILE ILE A . n 
A 1 254 ASN 254 255 255 ASN ASN A . n 
A 1 255 GLU 255 256 256 GLU GLU A . n 
A 1 256 THR 256 257 257 THR THR A . n 
A 1 257 HIS 257 258 258 HIS HIS A . n 
A 1 258 GLN 258 259 259 GLN GLN A . n 
A 1 259 GLY 259 260 260 GLY GLY A . n 
A 1 260 ARG 260 261 261 ARG ARG A . n 
A 1 261 TYR 261 262 262 TYR TYR A . n 
A 1 262 GLN 262 263 263 GLN GLN A . n 
A 1 263 VAL 263 264 264 VAL VAL A . n 
A 1 264 ASN 264 265 265 ASN ASN A . n 
A 1 265 THR 265 266 266 THR THR A . n 
A 1 266 MET 266 267 267 MET MET A . n 
A 1 267 TYR 267 268 268 TYR TYR A . n 
A 1 268 GLN 268 269 269 GLN GLN A . n 
A 1 269 ALA 269 270 270 ALA ALA A . n 
A 1 270 LEU 270 271 271 LEU LEU A . n 
A 1 271 GLY 271 272 272 GLY GLY A . n 
A 1 272 TRP 272 273 273 TRP TRP A . n 
A 1 273 GLU 273 274 274 GLU GLU A . n 
A 1 274 GLU 274 275 275 GLU GLU A . n 
A 1 275 PHE 275 276 276 PHE PHE A . n 
A 1 276 SER 276 277 277 SER SER A . n 
A 1 277 TYR 277 278 278 TYR TYR A . n 
A 1 278 PRO 278 279 279 PRO PRO A . n 
A 1 279 ALA 279 280 280 ALA ALA A . n 
A 1 280 THR 280 281 281 THR THR A . n 
A 1 281 LEU 281 282 282 LEU LEU A . n 
A 1 282 GLN 282 283 283 GLN GLN A . n 
A 1 283 THR 283 284 284 THR THR A . n 
A 1 284 LEU 284 285 285 LEU LEU A . n 
A 1 285 LEU 285 286 286 LEU LEU A . n 
A 1 286 ASP 286 287 287 ASP ASP A . n 
A 1 287 SER 287 288 288 SER SER A . n 
A 1 288 ASN 288 289 289 ASN ASN A . n 
A 1 289 SER 289 290 290 SER SER A . n 
A 1 290 GLU 290 291 291 GLU GLU A . n 
A 1 291 GLN 291 292 292 GLN GLN A . n 
A 1 292 ILE 292 293 293 ILE ILE A . n 
A 1 293 PHE 293 294 294 PHE PHE A . n 
A 1 294 MET 294 295 295 MET MET A . n 
A 1 295 LYS 295 296 296 LYS LYS A . n 
A 1 296 PRO 296 297 297 PRO PRO A . n 
A 1 297 ASN 297 298 298 ASN ASN A . n 
A 1 298 LYS 298 299 299 LYS LYS A . n 
A 1 299 VAL 299 300 300 VAL VAL A . n 
A 1 300 THR 300 301 301 THR THR A . n 
A 1 301 ALA 301 302 302 ALA ALA A . n 
A 1 302 ILE 302 303 303 ILE ILE A . n 
A 1 303 SER 303 304 304 SER SER A . n 
A 1 304 LYS 304 305 305 LYS LYS A . n 
A 1 305 GLU 305 306 306 GLU GLU A . n 
A 1 306 PRO 306 307 307 PRO PRO A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 VAL 308 309 309 VAL VAL A . n 
A 1 309 LYS 309 310 310 LYS LYS A . n 
A 1 310 MET 310 311 311 MET MET A . n 
A 1 311 TYR 311 312 312 TYR TYR A . n 
A 1 312 HIS 312 313 313 HIS HIS A . n 
A 1 313 LYS 313 314 314 LYS LYS A . n 
A 1 314 THR 314 315 315 THR THR A . n 
A 1 315 GLY 315 316 316 GLY GLY A . n 
A 1 316 THR 316 317 317 THR THR A . n 
A 1 317 THR 317 318 318 THR THR A . n 
A 1 318 ASN 318 319 319 ASN ASN A . n 
A 1 319 ARG 319 320 320 ARG ARG A . n 
A 1 320 SER 320 321 321 SER SER A . n 
A 1 321 GLY 321 322 322 GLY GLY A . n 
A 1 322 THR 322 323 323 THR THR A . n 
A 1 323 TYR 323 324 324 TYR TYR A . n 
A 1 324 VAL 324 325 325 VAL VAL A . n 
A 1 325 VAL 325 326 326 VAL VAL A . n 
A 1 326 PHE 326 327 327 PHE PHE A . n 
A 1 327 ILE 327 328 328 ILE ILE A . n 
A 1 328 PRO 328 329 329 PRO PRO A . n 
A 1 329 LYS 329 330 330 LYS LYS A . n 
A 1 330 GLU 330 331 331 GLU GLU A . n 
A 1 331 ASN 331 332 332 ASN ASN A . n 
A 1 332 ILE 332 333 333 ILE ILE A . n 
A 1 333 GLY 333 334 334 GLY GLY A . n 
A 1 334 LEU 334 335 335 LEU LEU A . n 
A 1 335 VAL 335 336 336 VAL VAL A . n 
A 1 336 MET 336 337 337 MET MET A . n 
A 1 337 LEU 337 338 338 LEU LEU A . n 
A 1 338 THR 338 339 339 THR THR A . n 
A 1 339 ASN 339 340 340 ASN ASN A . n 
A 1 340 LYS 340 341 341 LYS LYS A . n 
A 1 341 ARG 341 342 342 ARG ARG A . n 
A 1 342 ILE 342 343 343 ILE ILE A . n 
A 1 343 PRO 343 344 344 PRO PRO A . n 
A 1 344 ASN 344 345 345 ASN ASN A . n 
A 1 345 GLU 345 346 346 GLU GLU A . n 
A 1 346 GLU 346 347 347 GLU GLU A . n 
A 1 347 ARG 347 348 348 ARG ARG A . n 
A 1 348 ILE 348 349 349 ILE ILE A . n 
A 1 349 LYS 349 350 350 LYS LYS A . n 
A 1 350 ALA 350 351 351 ALA ALA A . n 
A 1 351 ALA 351 352 352 ALA ALA A . n 
A 1 352 TYR 352 353 353 TYR TYR A . n 
A 1 353 ALA 353 354 354 ALA ALA A . n 
A 1 354 VAL 354 355 355 VAL VAL A . n 
A 1 355 LEU 355 356 356 LEU LEU A . n 
A 1 356 ASN 356 357 357 ASN ASN A . n 
A 1 357 ALA 357 358 358 ALA ALA A . n 
A 1 358 ILE 358 359 359 ILE ILE A . n 
A 1 359 LYS 359 360 360 LYS LYS A . n 
A 1 360 LYS 360 361 361 LYS LYS A . n 
B 1 1   GLY 1   2   ?   ?   ?   B . n 
B 1 2   ASN 2   3   3   ASN ASN B . n 
B 1 3   THR 3   4   4   THR THR B . n 
B 1 4   PRO 4   5   5   PRO PRO B . n 
B 1 5   LYS 5   6   6   LYS LYS B . n 
B 1 6   ASP 6   7   7   ASP ASP B . n 
B 1 7   GLN 7   8   8   GLN GLN B . n 
B 1 8   GLU 8   9   9   GLU GLU B . n 
B 1 9   ILE 9   10  10  ILE ILE B . n 
B 1 10  LYS 10  11  11  LYS LYS B . n 
B 1 11  LYS 11  12  12  LYS LYS B . n 
B 1 12  LEU 12  13  13  LEU LEU B . n 
B 1 13  VAL 13  14  14  VAL VAL B . n 
B 1 14  ASP 14  15  15  ASP ASP B . n 
B 1 15  GLN 15  16  16  GLN GLN B . n 
B 1 16  ASN 16  17  17  ASN ASN B . n 
B 1 17  PHE 17  18  18  PHE PHE B . n 
B 1 18  LYS 18  19  19  LYS LYS B . n 
B 1 19  PRO 19  20  20  PRO PRO B . n 
B 1 20  LEU 20  21  21  LEU LEU B . n 
B 1 21  LEU 21  22  22  LEU LEU B . n 
B 1 22  GLU 22  23  23  GLU GLU B . n 
B 1 23  LYS 23  24  24  LYS LYS B . n 
B 1 24  TYR 24  25  25  TYR TYR B . n 
B 1 25  ASP 25  26  26  ASP ASP B . n 
B 1 26  VAL 26  27  27  VAL VAL B . n 
B 1 27  PRO 27  28  28  PRO PRO B . n 
B 1 28  GLY 28  29  29  GLY GLY B . n 
B 1 29  MET 29  30  30  MET MET B . n 
B 1 30  ALA 30  31  31  ALA ALA B . n 
B 1 31  VAL 31  32  32  VAL VAL B . n 
B 1 32  GLY 32  33  33  GLY GLY B . n 
B 1 33  VAL 33  34  34  VAL VAL B . n 
B 1 34  ILE 34  35  35  ILE ILE B . n 
B 1 35  GLN 35  36  36  GLN GLN B . n 
B 1 36  ASN 36  37  37  ASN ASN B . n 
B 1 37  ASN 37  38  38  ASN ASN B . n 
B 1 38  LYS 38  39  39  LYS LYS B . n 
B 1 39  LYS 39  40  40  LYS LYS B . n 
B 1 40  TYR 40  41  41  TYR TYR B . n 
B 1 41  GLU 41  42  42  GLU GLU B . n 
B 1 42  MET 42  43  43  MET MET B . n 
B 1 43  TYR 43  44  44  TYR TYR B . n 
B 1 44  TYR 44  45  45  TYR TYR B . n 
B 1 45  GLY 45  46  46  GLY GLY B . n 
B 1 46  LEU 46  47  47  LEU LEU B . n 
B 1 47  GLN 47  48  48  GLN GLN B . n 
B 1 48  SER 48  49  49  SER SER B . n 
B 1 49  VAL 49  50  50  VAL VAL B . n 
B 1 50  GLN 50  51  51  GLN GLN B . n 
B 1 51  ASP 51  52  52  ASP ASP B . n 
B 1 52  LYS 52  53  53  LYS LYS B . n 
B 1 53  LYS 53  54  54  LYS LYS B . n 
B 1 54  ALA 54  55  55  ALA ALA B . n 
B 1 55  VAL 55  56  56  VAL VAL B . n 
B 1 56  ASN 56  57  57  ASN ASN B . n 
B 1 57  SER 57  58  58  SER SER B . n 
B 1 58  SER 58  59  59  SER SER B . n 
B 1 59  THR 59  60  60  THR THR B . n 
B 1 60  ILE 60  61  61  ILE ILE B . n 
B 1 61  PHE 61  62  62  PHE PHE B . n 
B 1 62  GLU 62  63  63  GLU GLU B . n 
B 1 63  LEU 63  64  64  LEU LEU B . n 
B 1 64  GLY 64  65  65  GLY GLY B . n 
B 1 65  SER 65  66  66  SER SER B . n 
B 1 66  VAL 66  67  67  VAL VAL B . n 
B 1 67  SER 67  68  68  SER SER B . n 
B 1 68  LYS 68  69  69  LYS LYS B . n 
B 1 69  LEU 69  70  70  LEU LEU B . n 
B 1 70  PHE 70  71  71  PHE PHE B . n 
B 1 71  THR 71  72  72  THR THR B . n 
B 1 72  ALA 72  73  73  ALA ALA B . n 
B 1 73  THR 73  74  74  THR THR B . n 
B 1 74  ALA 74  75  75  ALA ALA B . n 
B 1 75  GLY 75  76  76  GLY GLY B . n 
B 1 76  GLY 76  77  77  GLY GLY B . n 
B 1 77  TYR 77  78  78  TYR TYR B . n 
B 1 78  ALA 78  79  79  ALA ALA B . n 
B 1 79  LYS 79  80  80  LYS LYS B . n 
B 1 80  ASN 80  81  81  ASN ASN B . n 
B 1 81  LYS 81  82  82  LYS LYS B . n 
B 1 82  GLY 82  83  83  GLY GLY B . n 
B 1 83  LYS 83  84  84  LYS LYS B . n 
B 1 84  ILE 84  85  85  ILE ILE B . n 
B 1 85  SER 85  86  86  SER SER B . n 
B 1 86  PHE 86  87  87  PHE PHE B . n 
B 1 87  ASP 87  88  88  ASP ASP B . n 
B 1 88  ASP 88  89  89  ASP ASP B . n 
B 1 89  THR 89  90  90  THR THR B . n 
B 1 90  PRO 90  91  91  PRO PRO B . n 
B 1 91  GLY 91  92  92  GLY GLY B . n 
B 1 92  LYS 92  93  93  LYS LYS B . n 
B 1 93  TYR 93  94  94  TYR TYR B . n 
B 1 94  TRP 94  95  95  TRP TRP B . n 
B 1 95  LYS 95  96  96  LYS LYS B . n 
B 1 96  GLU 96  97  97  GLU GLU B . n 
B 1 97  LEU 97  98  98  LEU LEU B . n 
B 1 98  LYS 98  99  99  LYS LYS B . n 
B 1 99  ASN 99  100 100 ASN ASN B . n 
B 1 100 THR 100 101 101 THR THR B . n 
B 1 101 PRO 101 102 102 PRO PRO B . n 
B 1 102 ILE 102 103 103 ILE ILE B . n 
B 1 103 ASP 103 104 104 ASP ASP B . n 
B 1 104 GLN 104 105 105 GLN GLN B . n 
B 1 105 VAL 105 106 106 VAL VAL B . n 
B 1 106 ASN 106 107 107 ASN ASN B . n 
B 1 107 LEU 107 108 108 LEU LEU B . n 
B 1 108 LEU 108 109 109 LEU LEU B . n 
B 1 109 GLN 109 110 110 GLN GLN B . n 
B 1 110 LEU 110 111 111 LEU LEU B . n 
B 1 111 ALA 111 112 112 ALA ALA B . n 
B 1 112 THR 112 113 113 THR THR B . n 
B 1 113 TYR 113 114 114 TYR TYR B . n 
B 1 114 THR 114 115 115 THR THR B . n 
B 1 115 SER 115 116 116 SER SER B . n 
B 1 116 GLY 116 117 117 GLY GLY B . n 
B 1 117 ASN 117 118 118 ASN ASN B . n 
B 1 118 LEU 118 119 119 LEU LEU B . n 
B 1 119 ALA 119 120 120 ALA ALA B . n 
B 1 120 LEU 120 121 121 LEU LEU B . n 
B 1 121 GLN 121 122 122 GLN GLN B . n 
B 1 122 PHE 122 123 123 PHE PHE B . n 
B 1 123 PRO 123 124 124 PRO PRO B . n 
B 1 124 ASP 124 125 125 ASP ASP B . n 
B 1 125 GLU 125 126 126 GLU GLU B . n 
B 1 126 VAL 126 127 127 VAL VAL B . n 
B 1 127 LYS 127 128 128 LYS LYS B . n 
B 1 128 THR 128 129 129 THR THR B . n 
B 1 129 ASP 129 130 130 ASP ASP B . n 
B 1 130 GLN 130 131 131 GLN GLN B . n 
B 1 131 GLN 131 132 132 GLN GLN B . n 
B 1 132 VAL 132 133 133 VAL VAL B . n 
B 1 133 LEU 133 134 134 LEU LEU B . n 
B 1 134 THR 134 135 135 THR THR B . n 
B 1 135 PHE 135 136 136 PHE PHE B . n 
B 1 136 PHE 136 137 137 PHE PHE B . n 
B 1 137 LYS 137 138 138 LYS LYS B . n 
B 1 138 ASP 138 139 139 ASP ASP B . n 
B 1 139 TRP 139 140 140 TRP TRP B . n 
B 1 140 LYS 140 141 141 LYS LYS B . n 
B 1 141 PRO 141 142 142 PRO PRO B . n 
B 1 142 LYS 142 143 143 LYS LYS B . n 
B 1 143 ASN 143 144 144 ASN ASN B . n 
B 1 144 SER 144 145 145 SER SER B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 GLY 146 147 147 GLY GLY B . n 
B 1 147 GLU 147 148 148 GLU GLU B . n 
B 1 148 TYR 148 149 149 TYR TYR B . n 
B 1 149 ARG 149 150 150 ARG ARG B . n 
B 1 150 GLN 150 151 151 GLN GLN B . n 
B 1 151 TYR 151 152 152 TYR TYR B . n 
B 1 152 SER 152 153 153 SER SER B . n 
B 1 153 ASN 153 154 154 ASN ASN B . n 
B 1 154 PRO 154 155 155 PRO PRO B . n 
B 1 155 SER 155 156 156 SER SER B . n 
B 1 156 ILE 156 157 157 ILE ILE B . n 
B 1 157 GLY 157 158 158 GLY GLY B . n 
B 1 158 LEU 158 159 159 LEU LEU B . n 
B 1 159 PHE 159 160 160 PHE PHE B . n 
B 1 160 GLY 160 161 161 GLY GLY B . n 
B 1 161 LYS 161 162 162 LYS LYS B . n 
B 1 162 VAL 162 163 163 VAL VAL B . n 
B 1 163 VAL 163 164 164 VAL VAL B . n 
B 1 164 ALA 164 165 165 ALA ALA B . n 
B 1 165 LEU 165 166 166 LEU LEU B . n 
B 1 166 SER 166 167 167 SER SER B . n 
B 1 167 MET 167 168 168 MET MET B . n 
B 1 168 ASN 168 169 169 ASN ASN B . n 
B 1 169 LYS 169 170 170 LYS LYS B . n 
B 1 170 PRO 170 171 171 PRO PRO B . n 
B 1 171 PHE 171 172 172 PHE PHE B . n 
B 1 172 ASP 172 173 173 ASP ASP B . n 
B 1 173 GLN 173 174 174 GLN GLN B . n 
B 1 174 VAL 174 175 175 VAL VAL B . n 
B 1 175 LEU 175 176 176 LEU LEU B . n 
B 1 176 GLU 176 177 177 GLU GLU B . n 
B 1 177 LYS 177 178 178 LYS LYS B . n 
B 1 178 THR 178 179 179 THR THR B . n 
B 1 179 ILE 179 180 180 ILE ILE B . n 
B 1 180 PHE 180 181 181 PHE PHE B . n 
B 1 181 PRO 181 182 182 PRO PRO B . n 
B 1 182 ALA 182 183 183 ALA ALA B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 GLY 184 185 185 GLY GLY B . n 
B 1 185 LEU 185 186 186 LEU LEU B . n 
B 1 186 LYS 186 187 187 LYS LYS B . n 
B 1 187 HIS 187 188 188 HIS HIS B . n 
B 1 188 SER 188 189 189 SER SER B . n 
B 1 189 TYR 189 190 190 TYR TYR B . n 
B 1 190 VAL 190 191 191 VAL VAL B . n 
B 1 191 ASN 191 192 192 ASN ASN B . n 
B 1 192 VAL 192 193 193 VAL VAL B . n 
B 1 193 PRO 193 194 194 PRO PRO B . n 
B 1 194 LYS 194 195 195 LYS LYS B . n 
B 1 195 THR 195 196 196 THR THR B . n 
B 1 196 GLN 196 197 197 GLN GLN B . n 
B 1 197 MET 197 198 198 MET MET B . n 
B 1 198 GLN 198 199 199 GLN GLN B . n 
B 1 199 ASN 199 200 200 ASN ASN B . n 
B 1 200 TYR 200 201 201 TYR TYR B . n 
B 1 201 ALA 201 202 202 ALA ALA B . n 
B 1 202 PHE 202 203 203 PHE PHE B . n 
B 1 203 GLY 203 204 204 GLY GLY B . n 
B 1 204 TYR 204 205 205 TYR TYR B . n 
B 1 205 ASN 205 206 206 ASN ASN B . n 
B 1 206 GLN 206 207 207 GLN GLN B . n 
B 1 207 GLU 207 208 208 GLU GLU B . n 
B 1 208 ASN 208 209 209 ASN ASN B . n 
B 1 209 GLN 209 210 210 GLN GLN B . n 
B 1 210 PRO 210 211 211 PRO PRO B . n 
B 1 211 ILE 211 212 212 ILE ILE B . n 
B 1 212 ARG 212 213 ?   ?   ?   B . n 
B 1 213 VAL 213 214 ?   ?   ?   B . n 
B 1 214 ASN 214 215 ?   ?   ?   B . n 
B 1 215 PRO 215 216 ?   ?   ?   B . n 
B 1 216 GLY 216 217 217 GLY GLY B . n 
B 1 217 PRO 217 218 218 PRO PRO B . n 
B 1 218 LEU 218 219 219 LEU LEU B . n 
B 1 219 GLY 219 220 220 GLY GLY B . n 
B 1 220 ALA 220 221 221 ALA ALA B . n 
B 1 221 PRO 221 222 222 PRO PRO B . n 
B 1 222 ALA 222 223 223 ALA ALA B . n 
B 1 223 TYR 223 224 224 TYR TYR B . n 
B 1 224 GLY 224 225 225 GLY GLY B . n 
B 1 225 VAL 225 226 226 VAL VAL B . n 
B 1 226 LYS 226 227 227 LYS LYS B . n 
B 1 227 SER 227 228 228 SER SER B . n 
B 1 228 THR 228 229 229 THR THR B . n 
B 1 229 LEU 229 230 230 LEU LEU B . n 
B 1 230 PRO 230 231 231 PRO PRO B . n 
B 1 231 ASP 231 232 232 ASP ASP B . n 
B 1 232 MET 232 233 233 MET MET B . n 
B 1 233 LEU 233 234 234 LEU LEU B . n 
B 1 234 SER 234 235 235 SER SER B . n 
B 1 235 PHE 235 236 236 PHE PHE B . n 
B 1 236 ILE 236 237 237 ILE ILE B . n 
B 1 237 HIS 237 238 238 HIS HIS B . n 
B 1 238 ALA 238 239 239 ALA ALA B . n 
B 1 239 ASN 239 240 240 ASN ASN B . n 
B 1 240 LEU 240 241 241 LEU LEU B . n 
B 1 241 ASN 241 242 242 ASN ASN B . n 
B 1 242 PRO 242 243 243 PRO PRO B . n 
B 1 243 GLN 243 244 244 GLN GLN B . n 
B 1 244 LYS 244 245 245 LYS LYS B . n 
B 1 245 TYR 245 246 246 TYR TYR B . n 
B 1 246 PRO 246 247 247 PRO PRO B . n 
B 1 247 ALA 247 248 248 ALA ALA B . n 
B 1 248 ASP 248 249 249 ASP ASP B . n 
B 1 249 ILE 249 250 250 ILE ILE B . n 
B 1 250 GLN 250 251 251 GLN GLN B . n 
B 1 251 ARG 251 252 252 ARG ARG B . n 
B 1 252 ALA 252 253 253 ALA ALA B . n 
B 1 253 ILE 253 254 254 ILE ILE B . n 
B 1 254 ASN 254 255 255 ASN ASN B . n 
B 1 255 GLU 255 256 256 GLU GLU B . n 
B 1 256 THR 256 257 257 THR THR B . n 
B 1 257 HIS 257 258 258 HIS HIS B . n 
B 1 258 GLN 258 259 259 GLN GLN B . n 
B 1 259 GLY 259 260 260 GLY GLY B . n 
B 1 260 ARG 260 261 261 ARG ARG B . n 
B 1 261 TYR 261 262 262 TYR TYR B . n 
B 1 262 GLN 262 263 263 GLN GLN B . n 
B 1 263 VAL 263 264 264 VAL VAL B . n 
B 1 264 ASN 264 265 265 ASN ASN B . n 
B 1 265 THR 265 266 266 THR THR B . n 
B 1 266 MET 266 267 267 MET MET B . n 
B 1 267 TYR 267 268 268 TYR TYR B . n 
B 1 268 GLN 268 269 269 GLN GLN B . n 
B 1 269 ALA 269 270 270 ALA ALA B . n 
B 1 270 LEU 270 271 271 LEU LEU B . n 
B 1 271 GLY 271 272 272 GLY GLY B . n 
B 1 272 TRP 272 273 273 TRP TRP B . n 
B 1 273 GLU 273 274 274 GLU GLU B . n 
B 1 274 GLU 274 275 275 GLU GLU B . n 
B 1 275 PHE 275 276 276 PHE PHE B . n 
B 1 276 SER 276 277 277 SER SER B . n 
B 1 277 TYR 277 278 278 TYR TYR B . n 
B 1 278 PRO 278 279 279 PRO PRO B . n 
B 1 279 ALA 279 280 280 ALA ALA B . n 
B 1 280 THR 280 281 281 THR THR B . n 
B 1 281 LEU 281 282 282 LEU LEU B . n 
B 1 282 GLN 282 283 283 GLN GLN B . n 
B 1 283 THR 283 284 284 THR THR B . n 
B 1 284 LEU 284 285 285 LEU LEU B . n 
B 1 285 LEU 285 286 286 LEU LEU B . n 
B 1 286 ASP 286 287 287 ASP ASP B . n 
B 1 287 SER 287 288 288 SER SER B . n 
B 1 288 ASN 288 289 289 ASN ASN B . n 
B 1 289 SER 289 290 290 SER SER B . n 
B 1 290 GLU 290 291 291 GLU GLU B . n 
B 1 291 GLN 291 292 292 GLN GLN B . n 
B 1 292 ILE 292 293 293 ILE ILE B . n 
B 1 293 PHE 293 294 294 PHE PHE B . n 
B 1 294 MET 294 295 295 MET MET B . n 
B 1 295 LYS 295 296 296 LYS LYS B . n 
B 1 296 PRO 296 297 297 PRO PRO B . n 
B 1 297 ASN 297 298 298 ASN ASN B . n 
B 1 298 LYS 298 299 299 LYS LYS B . n 
B 1 299 VAL 299 300 300 VAL VAL B . n 
B 1 300 THR 300 301 301 THR THR B . n 
B 1 301 ALA 301 302 302 ALA ALA B . n 
B 1 302 ILE 302 303 303 ILE ILE B . n 
B 1 303 SER 303 304 304 SER SER B . n 
B 1 304 LYS 304 305 305 LYS LYS B . n 
B 1 305 GLU 305 306 306 GLU GLU B . n 
B 1 306 PRO 306 307 307 PRO PRO B . n 
B 1 307 SER 307 308 308 SER SER B . n 
B 1 308 VAL 308 309 309 VAL VAL B . n 
B 1 309 LYS 309 310 310 LYS LYS B . n 
B 1 310 MET 310 311 311 MET MET B . n 
B 1 311 TYR 311 312 312 TYR TYR B . n 
B 1 312 HIS 312 313 313 HIS HIS B . n 
B 1 313 LYS 313 314 314 LYS LYS B . n 
B 1 314 THR 314 315 315 THR THR B . n 
B 1 315 GLY 315 316 316 GLY GLY B . n 
B 1 316 THR 316 317 317 THR THR B . n 
B 1 317 THR 317 318 318 THR THR B . n 
B 1 318 ASN 318 319 319 ASN ASN B . n 
B 1 319 ARG 319 320 320 ARG ARG B . n 
B 1 320 SER 320 321 321 SER SER B . n 
B 1 321 GLY 321 322 322 GLY GLY B . n 
B 1 322 THR 322 323 323 THR THR B . n 
B 1 323 TYR 323 324 324 TYR TYR B . n 
B 1 324 VAL 324 325 325 VAL VAL B . n 
B 1 325 VAL 325 326 326 VAL VAL B . n 
B 1 326 PHE 326 327 327 PHE PHE B . n 
B 1 327 ILE 327 328 328 ILE ILE B . n 
B 1 328 PRO 328 329 329 PRO PRO B . n 
B 1 329 LYS 329 330 330 LYS LYS B . n 
B 1 330 GLU 330 331 331 GLU GLU B . n 
B 1 331 ASN 331 332 332 ASN ASN B . n 
B 1 332 ILE 332 333 333 ILE ILE B . n 
B 1 333 GLY 333 334 334 GLY GLY B . n 
B 1 334 LEU 334 335 335 LEU LEU B . n 
B 1 335 VAL 335 336 336 VAL VAL B . n 
B 1 336 MET 336 337 337 MET MET B . n 
B 1 337 LEU 337 338 338 LEU LEU B . n 
B 1 338 THR 338 339 339 THR THR B . n 
B 1 339 ASN 339 340 340 ASN ASN B . n 
B 1 340 LYS 340 341 341 LYS LYS B . n 
B 1 341 ARG 341 342 342 ARG ARG B . n 
B 1 342 ILE 342 343 343 ILE ILE B . n 
B 1 343 PRO 343 344 344 PRO PRO B . n 
B 1 344 ASN 344 345 345 ASN ASN B . n 
B 1 345 GLU 345 346 346 GLU GLU B . n 
B 1 346 GLU 346 347 347 GLU GLU B . n 
B 1 347 ARG 347 348 348 ARG ARG B . n 
B 1 348 ILE 348 349 349 ILE ILE B . n 
B 1 349 LYS 349 350 350 LYS LYS B . n 
B 1 350 ALA 350 351 351 ALA ALA B . n 
B 1 351 ALA 351 352 352 ALA ALA B . n 
B 1 352 TYR 352 353 353 TYR TYR B . n 
B 1 353 ALA 353 354 354 ALA ALA B . n 
B 1 354 VAL 354 355 355 VAL VAL B . n 
B 1 355 LEU 355 356 356 LEU LEU B . n 
B 1 356 ASN 356 357 357 ASN ASN B . n 
B 1 357 ALA 357 358 358 ALA ALA B . n 
B 1 358 ILE 358 359 359 ILE ILE B . n 
B 1 359 LYS 359 360 ?   ?   ?   B . n 
B 1 360 LYS 360 361 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NO3 1   401 401 NO3 NO3 B . 
D 3 EDO 1   402 402 EDO EDO B . 
E 3 EDO 1   403 403 EDO EDO B . 
F 4 HOH 1   401 206 HOH HOH A . 
F 4 HOH 2   402 236 HOH HOH A . 
F 4 HOH 3   403 214 HOH HOH A . 
F 4 HOH 4   404 257 HOH HOH A . 
F 4 HOH 5   405 279 HOH HOH A . 
F 4 HOH 6   406 13  HOH HOH A . 
F 4 HOH 7   407 265 HOH HOH A . 
F 4 HOH 8   408 248 HOH HOH A . 
F 4 HOH 9   409 122 HOH HOH A . 
F 4 HOH 10  410 22  HOH HOH A . 
F 4 HOH 11  411 171 HOH HOH A . 
F 4 HOH 12  412 12  HOH HOH A . 
F 4 HOH 13  413 118 HOH HOH A . 
F 4 HOH 14  414 77  HOH HOH A . 
F 4 HOH 15  415 130 HOH HOH A . 
F 4 HOH 16  416 29  HOH HOH A . 
F 4 HOH 17  417 64  HOH HOH A . 
F 4 HOH 18  418 258 HOH HOH A . 
F 4 HOH 19  419 147 HOH HOH A . 
F 4 HOH 20  420 137 HOH HOH A . 
F 4 HOH 21  421 287 HOH HOH A . 
F 4 HOH 22  422 280 HOH HOH A . 
F 4 HOH 23  423 59  HOH HOH A . 
F 4 HOH 24  424 181 HOH HOH A . 
F 4 HOH 25  425 197 HOH HOH A . 
F 4 HOH 26  426 274 HOH HOH A . 
F 4 HOH 27  427 154 HOH HOH A . 
F 4 HOH 28  428 215 HOH HOH A . 
F 4 HOH 29  429 3   HOH HOH A . 
F 4 HOH 30  430 276 HOH HOH A . 
F 4 HOH 31  431 262 HOH HOH A . 
F 4 HOH 32  432 69  HOH HOH A . 
F 4 HOH 33  433 201 HOH HOH A . 
F 4 HOH 34  434 160 HOH HOH A . 
F 4 HOH 35  435 261 HOH HOH A . 
F 4 HOH 36  436 138 HOH HOH A . 
F 4 HOH 37  437 238 HOH HOH A . 
F 4 HOH 38  438 15  HOH HOH A . 
F 4 HOH 39  439 112 HOH HOH A . 
F 4 HOH 40  440 43  HOH HOH A . 
F 4 HOH 41  441 255 HOH HOH A . 
F 4 HOH 42  442 84  HOH HOH A . 
F 4 HOH 43  443 269 HOH HOH A . 
F 4 HOH 44  444 96  HOH HOH A . 
F 4 HOH 45  445 127 HOH HOH A . 
F 4 HOH 46  446 36  HOH HOH A . 
F 4 HOH 47  447 24  HOH HOH A . 
F 4 HOH 48  448 136 HOH HOH A . 
F 4 HOH 49  449 254 HOH HOH A . 
F 4 HOH 50  450 4   HOH HOH A . 
F 4 HOH 51  451 267 HOH HOH A . 
F 4 HOH 52  452 233 HOH HOH A . 
F 4 HOH 53  453 44  HOH HOH A . 
F 4 HOH 54  454 145 HOH HOH A . 
F 4 HOH 55  455 61  HOH HOH A . 
F 4 HOH 56  456 239 HOH HOH A . 
F 4 HOH 57  457 2   HOH HOH A . 
F 4 HOH 58  458 101 HOH HOH A . 
F 4 HOH 59  459 271 HOH HOH A . 
F 4 HOH 60  460 208 HOH HOH A . 
F 4 HOH 61  461 56  HOH HOH A . 
F 4 HOH 62  462 142 HOH HOH A . 
F 4 HOH 63  463 92  HOH HOH A . 
F 4 HOH 64  464 283 HOH HOH A . 
F 4 HOH 65  465 275 HOH HOH A . 
F 4 HOH 66  466 230 HOH HOH A . 
F 4 HOH 67  467 34  HOH HOH A . 
F 4 HOH 68  468 39  HOH HOH A . 
F 4 HOH 69  469 319 HOH HOH A . 
F 4 HOH 70  470 148 HOH HOH A . 
F 4 HOH 71  471 5   HOH HOH A . 
F 4 HOH 72  472 8   HOH HOH A . 
F 4 HOH 73  473 286 HOH HOH A . 
F 4 HOH 74  474 237 HOH HOH A . 
F 4 HOH 75  475 263 HOH HOH A . 
F 4 HOH 76  476 38  HOH HOH A . 
F 4 HOH 77  477 107 HOH HOH A . 
F 4 HOH 78  478 31  HOH HOH A . 
F 4 HOH 79  479 20  HOH HOH A . 
F 4 HOH 80  480 266 HOH HOH A . 
F 4 HOH 81  481 27  HOH HOH A . 
F 4 HOH 82  482 79  HOH HOH A . 
F 4 HOH 83  483 32  HOH HOH A . 
F 4 HOH 84  484 191 HOH HOH A . 
F 4 HOH 85  485 256 HOH HOH A . 
F 4 HOH 86  486 200 HOH HOH A . 
F 4 HOH 87  487 288 HOH HOH A . 
F 4 HOH 88  488 55  HOH HOH A . 
F 4 HOH 89  489 17  HOH HOH A . 
F 4 HOH 90  490 234 HOH HOH A . 
F 4 HOH 91  491 318 HOH HOH A . 
F 4 HOH 92  492 320 HOH HOH A . 
F 4 HOH 93  493 314 HOH HOH A . 
F 4 HOH 94  494 88  HOH HOH A . 
F 4 HOH 95  495 133 HOH HOH A . 
F 4 HOH 96  496 219 HOH HOH A . 
F 4 HOH 97  497 139 HOH HOH A . 
F 4 HOH 98  498 45  HOH HOH A . 
F 4 HOH 99  499 213 HOH HOH A . 
F 4 HOH 100 500 89  HOH HOH A . 
F 4 HOH 101 501 140 HOH HOH A . 
F 4 HOH 102 502 129 HOH HOH A . 
F 4 HOH 103 503 253 HOH HOH A . 
F 4 HOH 104 504 182 HOH HOH A . 
F 4 HOH 105 505 85  HOH HOH A . 
F 4 HOH 106 506 83  HOH HOH A . 
F 4 HOH 107 507 113 HOH HOH A . 
F 4 HOH 108 508 60  HOH HOH A . 
F 4 HOH 109 509 37  HOH HOH A . 
F 4 HOH 110 510 46  HOH HOH A . 
F 4 HOH 111 511 94  HOH HOH A . 
F 4 HOH 112 512 6   HOH HOH A . 
F 4 HOH 113 513 65  HOH HOH A . 
F 4 HOH 114 514 104 HOH HOH A . 
F 4 HOH 115 515 217 HOH HOH A . 
F 4 HOH 116 516 232 HOH HOH A . 
F 4 HOH 117 517 132 HOH HOH A . 
F 4 HOH 118 518 205 HOH HOH A . 
F 4 HOH 119 519 178 HOH HOH A . 
F 4 HOH 120 520 207 HOH HOH A . 
F 4 HOH 121 521 120 HOH HOH A . 
F 4 HOH 122 522 73  HOH HOH A . 
F 4 HOH 123 523 49  HOH HOH A . 
F 4 HOH 124 524 264 HOH HOH A . 
F 4 HOH 125 525 249 HOH HOH A . 
F 4 HOH 126 526 51  HOH HOH A . 
F 4 HOH 127 527 95  HOH HOH A . 
F 4 HOH 128 528 68  HOH HOH A . 
F 4 HOH 129 529 128 HOH HOH A . 
F 4 HOH 130 530 260 HOH HOH A . 
F 4 HOH 131 531 93  HOH HOH A . 
F 4 HOH 132 532 66  HOH HOH A . 
F 4 HOH 133 533 270 HOH HOH A . 
F 4 HOH 134 534 179 HOH HOH A . 
F 4 HOH 135 535 174 HOH HOH A . 
F 4 HOH 136 536 86  HOH HOH A . 
F 4 HOH 137 537 204 HOH HOH A . 
F 4 HOH 138 538 272 HOH HOH A . 
F 4 HOH 139 539 277 HOH HOH A . 
F 4 HOH 140 540 231 HOH HOH A . 
F 4 HOH 141 541 103 HOH HOH A . 
F 4 HOH 142 542 124 HOH HOH A . 
F 4 HOH 143 543 155 HOH HOH A . 
F 4 HOH 144 544 180 HOH HOH A . 
F 4 HOH 145 545 216 HOH HOH A . 
F 4 HOH 146 546 175 HOH HOH A . 
F 4 HOH 147 547 209 HOH HOH A . 
F 4 HOH 148 548 35  HOH HOH A . 
F 4 HOH 149 549 170 HOH HOH A . 
F 4 HOH 150 550 247 HOH HOH A . 
F 4 HOH 151 551 273 HOH HOH A . 
F 4 HOH 152 552 203 HOH HOH A . 
F 4 HOH 153 553 284 HOH HOH A . 
F 4 HOH 154 554 210 HOH HOH A . 
F 4 HOH 155 555 259 HOH HOH A . 
F 4 HOH 156 556 252 HOH HOH A . 
F 4 HOH 157 557 173 HOH HOH A . 
F 4 HOH 158 558 282 HOH HOH A . 
F 4 HOH 159 559 166 HOH HOH A . 
F 4 HOH 160 560 183 HOH HOH A . 
F 4 HOH 161 561 250 HOH HOH A . 
F 4 HOH 162 562 278 HOH HOH A . 
F 4 HOH 163 563 251 HOH HOH A . 
F 4 HOH 164 564 75  HOH HOH A . 
F 4 HOH 165 565 211 HOH HOH A . 
F 4 HOH 166 566 109 HOH HOH A . 
F 4 HOH 167 567 285 HOH HOH A . 
F 4 HOH 168 568 235 HOH HOH A . 
F 4 HOH 169 569 198 HOH HOH A . 
F 4 HOH 170 570 177 HOH HOH A . 
F 4 HOH 171 571 172 HOH HOH A . 
F 4 HOH 172 572 316 HOH HOH A . 
F 4 HOH 173 573 268 HOH HOH A . 
F 4 HOH 174 574 82  HOH HOH A . 
F 4 HOH 175 575 281 HOH HOH A . 
F 4 HOH 176 576 106 HOH HOH A . 
F 4 HOH 177 577 212 HOH HOH A . 
F 4 HOH 178 578 199 HOH HOH A . 
F 4 HOH 179 579 229 HOH HOH A . 
F 4 HOH 180 580 202 HOH HOH A . 
F 4 HOH 181 581 189 HOH HOH A . 
G 4 HOH 1   501 222 HOH HOH B . 
G 4 HOH 2   502 193 HOH HOH B . 
G 4 HOH 3   503 291 HOH HOH B . 
G 4 HOH 4   504 100 HOH HOH B . 
G 4 HOH 5   505 296 HOH HOH B . 
G 4 HOH 6   506 157 HOH HOH B . 
G 4 HOH 7   507 227 HOH HOH B . 
G 4 HOH 8   508 298 HOH HOH B . 
G 4 HOH 9   509 119 HOH HOH B . 
G 4 HOH 10  510 152 HOH HOH B . 
G 4 HOH 11  511 228 HOH HOH B . 
G 4 HOH 12  512 50  HOH HOH B . 
G 4 HOH 13  513 297 HOH HOH B . 
G 4 HOH 14  514 242 HOH HOH B . 
G 4 HOH 15  515 245 HOH HOH B . 
G 4 HOH 16  516 18  HOH HOH B . 
G 4 HOH 17  517 224 HOH HOH B . 
G 4 HOH 18  518 63  HOH HOH B . 
G 4 HOH 19  519 163 HOH HOH B . 
G 4 HOH 20  520 144 HOH HOH B . 
G 4 HOH 21  521 221 HOH HOH B . 
G 4 HOH 22  522 102 HOH HOH B . 
G 4 HOH 23  523 90  HOH HOH B . 
G 4 HOH 24  524 7   HOH HOH B . 
G 4 HOH 25  525 312 HOH HOH B . 
G 4 HOH 26  526 9   HOH HOH B . 
G 4 HOH 27  527 131 HOH HOH B . 
G 4 HOH 28  528 70  HOH HOH B . 
G 4 HOH 29  529 299 HOH HOH B . 
G 4 HOH 30  530 246 HOH HOH B . 
G 4 HOH 31  531 309 HOH HOH B . 
G 4 HOH 32  532 243 HOH HOH B . 
G 4 HOH 33  533 16  HOH HOH B . 
G 4 HOH 34  534 11  HOH HOH B . 
G 4 HOH 35  535 218 HOH HOH B . 
G 4 HOH 36  536 169 HOH HOH B . 
G 4 HOH 37  537 1   HOH HOH B . 
G 4 HOH 38  538 76  HOH HOH B . 
G 4 HOH 39  539 161 HOH HOH B . 
G 4 HOH 40  540 134 HOH HOH B . 
G 4 HOH 41  541 116 HOH HOH B . 
G 4 HOH 42  542 58  HOH HOH B . 
G 4 HOH 43  543 225 HOH HOH B . 
G 4 HOH 44  544 196 HOH HOH B . 
G 4 HOH 45  545 310 HOH HOH B . 
G 4 HOH 46  546 168 HOH HOH B . 
G 4 HOH 47  547 315 HOH HOH B . 
G 4 HOH 48  548 28  HOH HOH B . 
G 4 HOH 49  549 52  HOH HOH B . 
G 4 HOH 50  550 141 HOH HOH B . 
G 4 HOH 51  551 53  HOH HOH B . 
G 4 HOH 52  552 293 HOH HOH B . 
G 4 HOH 53  553 158 HOH HOH B . 
G 4 HOH 54  554 10  HOH HOH B . 
G 4 HOH 55  555 223 HOH HOH B . 
G 4 HOH 56  556 114 HOH HOH B . 
G 4 HOH 57  557 313 HOH HOH B . 
G 4 HOH 58  558 289 HOH HOH B . 
G 4 HOH 59  559 302 HOH HOH B . 
G 4 HOH 60  560 294 HOH HOH B . 
G 4 HOH 61  561 19  HOH HOH B . 
G 4 HOH 62  562 176 HOH HOH B . 
G 4 HOH 63  563 194 HOH HOH B . 
G 4 HOH 64  564 190 HOH HOH B . 
G 4 HOH 65  565 91  HOH HOH B . 
G 4 HOH 66  566 25  HOH HOH B . 
G 4 HOH 67  567 42  HOH HOH B . 
G 4 HOH 68  568 150 HOH HOH B . 
G 4 HOH 69  569 186 HOH HOH B . 
G 4 HOH 70  570 188 HOH HOH B . 
G 4 HOH 71  571 121 HOH HOH B . 
G 4 HOH 72  572 111 HOH HOH B . 
G 4 HOH 73  573 40  HOH HOH B . 
G 4 HOH 74  574 167 HOH HOH B . 
G 4 HOH 75  575 57  HOH HOH B . 
G 4 HOH 76  576 300 HOH HOH B . 
G 4 HOH 77  577 317 HOH HOH B . 
G 4 HOH 78  578 87  HOH HOH B . 
G 4 HOH 79  579 26  HOH HOH B . 
G 4 HOH 80  580 165 HOH HOH B . 
G 4 HOH 81  581 303 HOH HOH B . 
G 4 HOH 82  582 146 HOH HOH B . 
G 4 HOH 83  583 244 HOH HOH B . 
G 4 HOH 84  584 306 HOH HOH B . 
G 4 HOH 85  585 62  HOH HOH B . 
G 4 HOH 86  586 97  HOH HOH B . 
G 4 HOH 87  587 41  HOH HOH B . 
G 4 HOH 88  588 80  HOH HOH B . 
G 4 HOH 89  589 125 HOH HOH B . 
G 4 HOH 90  590 153 HOH HOH B . 
G 4 HOH 91  591 290 HOH HOH B . 
G 4 HOH 92  592 98  HOH HOH B . 
G 4 HOH 93  593 78  HOH HOH B . 
G 4 HOH 94  594 105 HOH HOH B . 
G 4 HOH 95  595 21  HOH HOH B . 
G 4 HOH 96  596 220 HOH HOH B . 
G 4 HOH 97  597 301 HOH HOH B . 
G 4 HOH 98  598 185 HOH HOH B . 
G 4 HOH 99  599 308 HOH HOH B . 
G 4 HOH 100 600 143 HOH HOH B . 
G 4 HOH 101 601 156 HOH HOH B . 
G 4 HOH 102 602 33  HOH HOH B . 
G 4 HOH 103 603 159 HOH HOH B . 
G 4 HOH 104 604 14  HOH HOH B . 
G 4 HOH 105 605 164 HOH HOH B . 
G 4 HOH 106 606 240 HOH HOH B . 
G 4 HOH 107 607 149 HOH HOH B . 
G 4 HOH 108 608 324 HOH HOH B . 
G 4 HOH 109 609 226 HOH HOH B . 
G 4 HOH 110 610 292 HOH HOH B . 
G 4 HOH 111 611 162 HOH HOH B . 
G 4 HOH 112 612 295 HOH HOH B . 
G 4 HOH 113 613 304 HOH HOH B . 
G 4 HOH 114 614 99  HOH HOH B . 
G 4 HOH 115 615 192 HOH HOH B . 
G 4 HOH 116 616 322 HOH HOH B . 
G 4 HOH 117 617 305 HOH HOH B . 
G 4 HOH 118 618 241 HOH HOH B . 
G 4 HOH 119 619 110 HOH HOH B . 
G 4 HOH 120 620 323 HOH HOH B . 
G 4 HOH 121 621 187 HOH HOH B . 
G 4 HOH 122 622 311 HOH HOH B . 
G 4 HOH 123 623 321 HOH HOH B . 
G 4 HOH 124 624 195 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.41 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MTV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.089 
_cell.length_a_esd                 ? 
_cell.length_b                     182.210 
_cell.length_b_esd                 ? 
_cell.length_c                     50.767 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MTV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MTV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.87 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M lithium chloride, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95369 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95369 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MTV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               38.64 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     70428 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.120 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3910 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.516 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.676 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MTV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             38.64 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     70294 
_refine.ls_number_reflns_R_free                  3399 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.59 
_refine.ls_percent_reflns_R_free                 4.84 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1885 
_refine.ls_R_factor_R_free                       0.2149 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1872 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.85 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.25 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        38.64 
_refine_hist.number_atoms_solvent             305 
_refine_hist.number_atoms_total               5981 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5664 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 5845 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.826  ? 7922 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.407 ? 2222 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 863  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1027 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.82  . . 116 2552 91.00  . . . . 0.3429 . . . . . . . . . . . 0.3423 
'X-RAY DIFFRACTION' 1.82 1.85  . . 143 2824 99.00  . . . . 0.3217 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 1.85 1.88  . . 134 2842 99.00  . . . . 0.2987 . . . . . . . . . . . 0.3118 
'X-RAY DIFFRACTION' 1.88 1.91  . . 146 2760 99.00  . . . . 0.2679 . . . . . . . . . . . 0.3517 
'X-RAY DIFFRACTION' 1.91 1.94  . . 164 2788 99.00  . . . . 0.2481 . . . . . . . . . . . 0.2605 
'X-RAY DIFFRACTION' 1.94 1.98  . . 135 2792 99.00  . . . . 0.2217 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 1.98 2.02  . . 124 2814 99.00  . . . . 0.2095 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 2.02 2.06  . . 141 2782 98.00  . . . . 0.2164 . . . . . . . . . . . 0.2849 
'X-RAY DIFFRACTION' 2.06 2.10  . . 137 2748 97.00  . . . . 0.2279 . . . . . . . . . . . 0.2817 
'X-RAY DIFFRACTION' 2.10 2.15  . . 132 2683 95.00  . . . . 0.2237 . . . . . . . . . . . 0.2865 
'X-RAY DIFFRACTION' 2.15 2.21  . . 123 2817 99.00  . . . . 0.2181 . . . . . . . . . . . 0.2447 
'X-RAY DIFFRACTION' 2.21 2.27  . . 160 2793 99.00  . . . . 0.1875 . . . . . . . . . . . 0.2215 
'X-RAY DIFFRACTION' 2.27 2.33  . . 146 2784 100.00 . . . . 0.1899 . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 2.33 2.41  . . 179 2811 100.00 . . . . 0.1882 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 2.41 2.49  . . 143 2774 99.00  . . . . 0.1820 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 2.49 2.59  . . 152 2799 99.00  . . . . 0.1940 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 2.59 2.71  . . 137 2796 98.00  . . . . 0.2003 . . . . . . . . . . . 0.2467 
'X-RAY DIFFRACTION' 2.71 2.85  . . 147 2782 98.00  . . . . 0.1993 . . . . . . . . . . . 0.2680 
'X-RAY DIFFRACTION' 2.85 3.03  . . 142 2819 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2273 
'X-RAY DIFFRACTION' 3.03 3.27  . . 160 2816 100.00 . . . . 0.1898 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 3.27 3.60  . . 143 2852 99.00  . . . . 0.1844 . . . . . . . . . . . 0.1952 
'X-RAY DIFFRACTION' 3.60 4.11  . . 135 2754 98.00  . . . . 0.1569 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 4.12 5.18  . . 124 2873 100.00 . . . . 0.1360 . . . . . . . . . . . 0.1415 
'X-RAY DIFFRACTION' 5.18 38.64 . . 136 2840 99.00  . . . . 0.1548 . . . . . . . . . . . 0.1507 
# 
_struct.entry_id                     9MTV 
_struct.title                        'Crystal structure of an apo-ADC-1 triple mutant' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9MTV 
_struct_keywords.text            'beta-lactamase, class C, apo-enzyme, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9L4R5_ACIBA 
_struct_ref.pdbx_db_accession          Q9L4R5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKEPSVKMYHKTGSTNRF
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_struct_ref.pdbx_align_begin           24 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9MTV A 1 ? 360 ? Q9L4R5 24 ? 383 ? 2 361 
2 1 9MTV B 1 ? 360 ? Q9L4R5 24 ? 383 ? 2 361 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9MTV PHE A 293 ? UNP Q9L4R5 VAL 316 'engineered mutation' 294 1 
1 9MTV THR A 316 ? UNP Q9L4R5 SER 339 'engineered mutation' 317 2 
1 9MTV SER A 320 ? UNP Q9L4R5 PHE 343 'engineered mutation' 321 3 
2 9MTV PHE B 293 ? UNP Q9L4R5 VAL 316 'engineered mutation' 294 4 
2 9MTV THR B 316 ? UNP Q9L4R5 SER 339 'engineered mutation' 317 5 
2 9MTV SER B 320 ? UNP Q9L4R5 PHE 343 'engineered mutation' 321 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,F       
2 1 B,C,D,E,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 3   ? PHE A 17  ? THR A 4   PHE A 18  1 ? 15 
HELX_P HELX_P2  AA2 PRO A 19  ? ASP A 25  ? PRO A 20  ASP A 26  1 ? 7  
HELX_P HELX_P3  AA3 GLY A 64  ? VAL A 66  ? GLY A 65  VAL A 67  5 ? 3  
HELX_P HELX_P4  AA4 SER A 67  ? LYS A 81  ? SER A 68  LYS A 82  1 ? 15 
HELX_P HELX_P5  AA5 THR A 89  ? TYR A 93  ? THR A 90  TYR A 94  5 ? 5  
HELX_P HELX_P6  AA6 TRP A 94  ? LYS A 98  ? TRP A 95  LYS A 99  5 ? 5  
HELX_P HELX_P7  AA7 THR A 100 ? VAL A 105 ? THR A 101 VAL A 106 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 106 ? THR A 112 ? ASN A 107 THR A 113 1 ? 7  
HELX_P HELX_P9  AA9 THR A 128 ? TRP A 139 ? THR A 129 TRP A 140 1 ? 12 
HELX_P HELX_P10 AB1 SER A 152 ? MET A 167 ? SER A 153 MET A 168 1 ? 16 
HELX_P HELX_P11 AB2 PRO A 170 ? THR A 178 ? PRO A 171 THR A 179 1 ? 9  
HELX_P HELX_P12 AB3 THR A 178 ? LEU A 183 ? THR A 179 LEU A 184 1 ? 6  
HELX_P HELX_P13 AB4 PRO A 193 ? TYR A 200 ? PRO A 194 TYR A 201 5 ? 8  
HELX_P HELX_P14 AB5 GLY A 219 ? GLY A 224 ? GLY A 220 GLY A 225 1 ? 6  
HELX_P HELX_P15 AB6 THR A 228 ? ASN A 241 ? THR A 229 ASN A 242 1 ? 14 
HELX_P HELX_P16 AB7 PRO A 242 ? TYR A 245 ? PRO A 243 TYR A 246 5 ? 4  
HELX_P HELX_P17 AB8 PRO A 246 ? THR A 256 ? PRO A 247 THR A 257 1 ? 11 
HELX_P HELX_P18 AB9 THR A 280 ? SER A 287 ? THR A 281 SER A 288 1 ? 8  
HELX_P HELX_P19 AC1 SER A 289 ? LYS A 295 ? SER A 290 LYS A 296 1 ? 7  
HELX_P HELX_P20 AC2 PRO A 328 ? GLU A 330 ? PRO A 329 GLU A 331 5 ? 3  
HELX_P HELX_P21 AC3 PRO A 343 ? ILE A 358 ? PRO A 344 ILE A 359 1 ? 16 
HELX_P HELX_P22 AC4 THR B 3   ? ASP B 25  ? THR B 4   ASP B 26  1 ? 23 
HELX_P HELX_P23 AC5 VAL B 66  ? LYS B 81  ? VAL B 67  LYS B 82  1 ? 16 
HELX_P HELX_P24 AC6 THR B 89  ? TYR B 93  ? THR B 90  TYR B 94  5 ? 5  
HELX_P HELX_P25 AC7 TRP B 94  ? LYS B 98  ? TRP B 95  LYS B 99  5 ? 5  
HELX_P HELX_P26 AC8 THR B 100 ? VAL B 105 ? THR B 101 VAL B 106 5 ? 6  
HELX_P HELX_P27 AC9 ASN B 106 ? THR B 112 ? ASN B 107 THR B 113 1 ? 7  
HELX_P HELX_P28 AD1 THR B 128 ? TRP B 139 ? THR B 129 TRP B 140 1 ? 12 
HELX_P HELX_P29 AD2 SER B 152 ? MET B 167 ? SER B 153 MET B 168 1 ? 16 
HELX_P HELX_P30 AD3 PRO B 170 ? THR B 178 ? PRO B 171 THR B 179 1 ? 9  
HELX_P HELX_P31 AD4 THR B 178 ? LEU B 183 ? THR B 179 LEU B 184 1 ? 6  
HELX_P HELX_P32 AD5 PRO B 193 ? TYR B 200 ? PRO B 194 TYR B 201 5 ? 8  
HELX_P HELX_P33 AD6 GLY B 219 ? GLY B 224 ? GLY B 220 GLY B 225 1 ? 6  
HELX_P HELX_P34 AD7 THR B 228 ? ASN B 241 ? THR B 229 ASN B 242 1 ? 14 
HELX_P HELX_P35 AD8 PRO B 242 ? TYR B 245 ? PRO B 243 TYR B 246 5 ? 4  
HELX_P HELX_P36 AD9 PRO B 246 ? THR B 256 ? PRO B 247 THR B 257 1 ? 11 
HELX_P HELX_P37 AE1 THR B 280 ? SER B 287 ? THR B 281 SER B 288 1 ? 8  
HELX_P HELX_P38 AE2 SER B 289 ? LYS B 295 ? SER B 290 LYS B 296 1 ? 7  
HELX_P HELX_P39 AE3 PRO B 328 ? GLU B 330 ? PRO B 329 GLU B 331 5 ? 3  
HELX_P HELX_P40 AE4 PRO B 343 ? ILE B 358 ? PRO B 344 ILE B 359 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 277 A . ? TYR 278 A PRO 278 A ? PRO 279 A 1 -5.82 
2 TYR 277 B . ? TYR 278 B PRO 278 B ? PRO 279 B 1 5.04  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 53  ? ALA A 54  ? LYS A 54  ALA A 55  
AA1 2 LYS A 38  ? SER A 48  ? LYS A 39  SER A 49  
AA1 3 GLY A 28  ? GLN A 35  ? GLY A 29  GLN A 36  
AA1 4 ILE A 332 ? THR A 338 ? ILE A 333 THR A 339 
AA1 5 GLY A 321 ? ILE A 327 ? GLY A 322 ILE A 328 
AA1 6 LYS A 309 ? THR A 314 ? LYS A 310 THR A 315 
AA1 7 GLU A 273 ? SER A 276 ? GLU A 274 SER A 277 
AA1 8 MET A 266 ? GLN A 268 ? MET A 267 GLN A 269 
AA1 9 TYR A 261 ? VAL A 263 ? TYR A 262 VAL A 264 
AA2 1 PHE A 61  ? GLU A 62  ? PHE A 62  GLU A 63  
AA2 2 LYS A 226 ? SER A 227 ? LYS A 227 SER A 228 
AA3 1 TYR A 148 ? ARG A 149 ? TYR A 149 ARG A 150 
AA3 2 ASN A 297 ? LYS A 298 ? ASN A 298 LYS A 299 
AA4 1 GLY A 203 ? TYR A 204 ? GLY A 204 TYR A 205 
AA4 2 PRO A 210 ? ILE A 211 ? PRO A 211 ILE A 212 
AA5 1 LYS B 38  ? GLY B 45  ? LYS B 39  GLY B 46  
AA5 2 GLY B 28  ? GLN B 35  ? GLY B 29  GLN B 36  
AA5 3 ILE B 332 ? THR B 338 ? ILE B 333 THR B 339 
AA5 4 SER B 320 ? ILE B 327 ? SER B 321 ILE B 328 
AA5 5 LYS B 309 ? THR B 317 ? LYS B 310 THR B 318 
AA5 6 GLU B 273 ? SER B 276 ? GLU B 274 SER B 277 
AA5 7 MET B 266 ? GLN B 268 ? MET B 267 GLN B 269 
AA5 8 TYR B 261 ? VAL B 263 ? TYR B 262 VAL B 264 
AA6 1 PHE B 61  ? GLU B 62  ? PHE B 62  GLU B 63  
AA6 2 LYS B 226 ? SER B 227 ? LYS B 227 SER B 228 
AA7 1 TYR B 148 ? ARG B 149 ? TYR B 149 ARG B 150 
AA7 2 ASN B 297 ? LYS B 298 ? ASN B 298 LYS B 299 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LYS A 53  ? O LYS A 54  N GLN A 47  ? N GLN A 48  
AA1 2 3 O MET A 42  ? O MET A 43  N VAL A 31  ? N VAL A 32  
AA1 3 4 N ALA A 30  ? N ALA A 31  O LEU A 337 ? O LEU A 338 
AA1 4 5 O MET A 336 ? O MET A 337 N TYR A 323 ? N TYR A 324 
AA1 5 6 O PHE A 326 ? O PHE A 327 N TYR A 311 ? N TYR A 312 
AA1 6 7 O MET A 310 ? O MET A 311 N PHE A 275 ? N PHE A 276 
AA1 7 8 O GLU A 274 ? O GLU A 275 N TYR A 267 ? N TYR A 268 
AA1 8 9 O MET A 266 ? O MET A 267 N VAL A 263 ? N VAL A 264 
AA2 1 2 N PHE A 61  ? N PHE A 62  O SER A 227 ? O SER A 228 
AA3 1 2 N ARG A 149 ? N ARG A 150 O ASN A 297 ? O ASN A 298 
AA4 1 2 N GLY A 203 ? N GLY A 204 O ILE A 211 ? O ILE A 212 
AA5 1 2 O LYS B 38  ? O LYS B 39  N GLN B 35  ? N GLN B 36  
AA5 2 3 N ALA B 30  ? N ALA B 31  O LEU B 337 ? O LEU B 338 
AA5 3 4 O ILE B 332 ? O ILE B 333 N ILE B 327 ? N ILE B 328 
AA5 4 5 O THR B 322 ? O THR B 323 N GLY B 315 ? N GLY B 316 
AA5 5 6 O MET B 310 ? O MET B 311 N PHE B 275 ? N PHE B 276 
AA5 6 7 O GLU B 274 ? O GLU B 275 N TYR B 267 ? N TYR B 268 
AA5 7 8 O MET B 266 ? O MET B 267 N VAL B 263 ? N VAL B 264 
AA6 1 2 N PHE B 61  ? N PHE B 62  O SER B 227 ? O SER B 228 
AA7 1 2 N ARG B 149 ? N ARG B 150 O ASN B 297 ? O ASN B 298 
# 
_pdbx_entry_details.entry_id                   9MTV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 118 ? ? -155.16 51.13   
2  1 LYS A 143 ? ? -124.03 -81.71  
3  1 TYR A 224 ? ? -154.74 23.53   
4  1 ASN A 265 ? ? 57.95   -121.56 
5  1 SER A 304 ? ? -73.38  -71.49  
6  1 THR A 317 ? ? -35.15  -97.12  
7  1 THR A 318 ? ? 45.61   -137.76 
8  1 ARG A 320 ? ? 59.94   6.31    
9  1 ASN B 118 ? ? -158.00 56.32   
10 1 LYS B 128 ? ? -126.29 -59.98  
11 1 LYS B 143 ? ? -117.93 -76.35  
12 1 THR B 179 ? ? -124.85 -55.25  
13 1 TYR B 224 ? ? -155.83 28.23   
14 1 ASN B 265 ? ? 55.35   -118.61 
15 1 SER B 304 ? ? -101.76 -63.06  
16 1 ARG B 320 ? ? -149.15 40.74   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 13.3037 -8.3038  11.8470 0.2930 ? 0.0187  ? 0.0083  ? 0.2275 ? 0.0067  ? 0.2876 ? 1.4204 ? -0.9324 
? 0.6371  ? 1.8895 ? 0.1339  ? 1.0688 ? -0.0877 ? -0.0744 ? 0.1894  ? 0.2483  ? -0.0393 ? 0.0981  ? -0.2574 ? -0.1942 ? -0.0003 ? 
2 'X-RAY DIFFRACTION' ? refined 23.7072 -27.9107 -8.1952 0.1923 ? 0.0083  ? -0.0101 ? 0.2093 ? 0.0191  ? 0.1466 ? 1.3786 ? -0.1506 
? -0.3564 ? 0.9384 ? 0.1333  ? 0.8645 ? 0.0626  ? 0.1019  ? 0.0634  ? -0.1782 ? -0.0067 ? -0.0113 ? -0.0781 ? -0.0506 ? 0.0005  ? 
3 'X-RAY DIFFRACTION' ? refined 22.1973 -28.2603 6.9646  0.1838 ? -0.0066 ? 0.0017  ? 0.2403 ? 0.0171  ? 0.1911 ? 1.0550 ? -0.6783 
? -0.1343 ? 1.5974 ? -0.0575 ? 1.1201 ? -0.0003 ? -0.1147 ? 0.1080  ? 0.0808  ? -0.0145 ? -0.1750 ? -0.0270 ? 0.0880  ? 0.0004  ? 
4 'X-RAY DIFFRACTION' ? refined 20.9356 -18.3692 13.0450 0.2796 ? 0.0036  ? 0.0012  ? 0.2642 ? 0.0112  ? 0.2536 ? 1.7147 ? -0.9873 
? 0.5804  ? 1.7576 ? 0.6104  ? 1.1356 ? 0.0306  ? -0.0374 ? 0.2160  ? 0.1387  ? -0.0431 ? -0.1829 ? -0.0125 ? 0.2202  ? 0.0001  ? 
5 'X-RAY DIFFRACTION' ? refined 2.4883  9.1897   -3.4580 0.3503 ? 0.0078  ? -0.0134 ? 0.2958 ? -0.0233 ? 0.3639 ? 0.4648 ? -0.2469 
? -0.3283 ? 1.5045 ? -0.0751 ? 0.7792 ? 0.0310  ? 0.2860  ? -0.2840 ? -0.3791 ? -0.0935 ? -0.0157 ? 0.2881  ? -0.1057 ? 0.0003  ? 
6 'X-RAY DIFFRACTION' ? refined -3.2744 25.7932  19.1968 0.4365 ? -0.0513 ? 0.0348  ? 0.2420 ? 0.0147  ? 0.1927 ? 0.8338 ? 0.1274  
? -0.1686 ? 2.9611 ? 0.0882  ? 0.2059 ? 0.0764  ? -0.1850 ? -0.0560 ? 1.0131  ? -0.1298 ? 0.2310  ? 0.0843  ? -0.0056 ? -0.0101 ? 
7 'X-RAY DIFFRACTION' ? refined -7.3345 32.0566  2.6359  0.2576 ? 0.0058  ? -0.0435 ? 0.2709 ? 0.0051  ? 0.2948 ? 0.2478 ? -0.4348 
? -0.0796 ? 2.7779 ? 0.5469  ? 0.3320 ? 0.0321  ? 0.0627  ? 0.0720  ? -0.2298 ? -0.1116 ? 0.3107  ? -0.0489 ? 0.0099  ? 0.0003  ? 
8 'X-RAY DIFFRACTION' ? refined 1.1631  20.7841  0.5746  0.2165 ? 0.0013  ? -0.0152 ? 0.2354 ? 0.0175  ? 0.2263 ? 0.8496 ? -0.0998 
? -0.6922 ? 2.5449 ? 0.2632  ? 0.7737 ? 0.0619  ? 0.1298  ? 0.0042  ? -0.1674 ? -0.1056 ? -0.1115 ? -0.0795 ? 0.0180  ? 0.0002  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 64 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 65 through 210 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 211 through 309 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 310 through 361 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 46 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 47 through 241 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 242 through 309 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 310 through 359 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       624 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.99 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 2   ? A GLY 1   
2 1 Y 1 B GLY 2   ? B GLY 1   
3 1 Y 1 B ARG 213 ? B ARG 212 
4 1 Y 1 B VAL 214 ? B VAL 213 
5 1 Y 1 B ASN 215 ? B ASN 214 
6 1 Y 1 B PRO 216 ? B PRO 215 
7 1 Y 1 B LYS 360 ? B LYS 359 
8 1 Y 1 B LYS 361 ? B LYS 360 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
EDO C1   C N N 74  
EDO O1   O N N 75  
EDO C2   C N N 76  
EDO O2   O N N 77  
EDO H11  H N N 78  
EDO H12  H N N 79  
EDO HO1  H N N 80  
EDO H21  H N N 81  
EDO H22  H N N 82  
EDO HO2  H N N 83  
GLN N    N N N 84  
GLN CA   C N S 85  
GLN C    C N N 86  
GLN O    O N N 87  
GLN CB   C N N 88  
GLN CG   C N N 89  
GLN CD   C N N 90  
GLN OE1  O N N 91  
GLN NE2  N N N 92  
GLN OXT  O N N 93  
GLN H    H N N 94  
GLN H2   H N N 95  
GLN HA   H N N 96  
GLN HB2  H N N 97  
GLN HB3  H N N 98  
GLN HG2  H N N 99  
GLN HG3  H N N 100 
GLN HE21 H N N 101 
GLN HE22 H N N 102 
GLN HXT  H N N 103 
GLU N    N N N 104 
GLU CA   C N S 105 
GLU C    C N N 106 
GLU O    O N N 107 
GLU CB   C N N 108 
GLU CG   C N N 109 
GLU CD   C N N 110 
GLU OE1  O N N 111 
GLU OE2  O N N 112 
GLU OXT  O N N 113 
GLU H    H N N 114 
GLU H2   H N N 115 
GLU HA   H N N 116 
GLU HB2  H N N 117 
GLU HB3  H N N 118 
GLU HG2  H N N 119 
GLU HG3  H N N 120 
GLU HE2  H N N 121 
GLU HXT  H N N 122 
GLY N    N N N 123 
GLY CA   C N N 124 
GLY C    C N N 125 
GLY O    O N N 126 
GLY OXT  O N N 127 
GLY H    H N N 128 
GLY H2   H N N 129 
GLY HA2  H N N 130 
GLY HA3  H N N 131 
GLY HXT  H N N 132 
HIS N    N N N 133 
HIS CA   C N S 134 
HIS C    C N N 135 
HIS O    O N N 136 
HIS CB   C N N 137 
HIS CG   C Y N 138 
HIS ND1  N Y N 139 
HIS CD2  C Y N 140 
HIS CE1  C Y N 141 
HIS NE2  N Y N 142 
HIS OXT  O N N 143 
HIS H    H N N 144 
HIS H2   H N N 145 
HIS HA   H N N 146 
HIS HB2  H N N 147 
HIS HB3  H N N 148 
HIS HD1  H N N 149 
HIS HD2  H N N 150 
HIS HE1  H N N 151 
HIS HE2  H N N 152 
HIS HXT  H N N 153 
HOH O    O N N 154 
HOH H1   H N N 155 
HOH H2   H N N 156 
ILE N    N N N 157 
ILE CA   C N S 158 
ILE C    C N N 159 
ILE O    O N N 160 
ILE CB   C N S 161 
ILE CG1  C N N 162 
ILE CG2  C N N 163 
ILE CD1  C N N 164 
ILE OXT  O N N 165 
ILE H    H N N 166 
ILE H2   H N N 167 
ILE HA   H N N 168 
ILE HB   H N N 169 
ILE HG12 H N N 170 
ILE HG13 H N N 171 
ILE HG21 H N N 172 
ILE HG22 H N N 173 
ILE HG23 H N N 174 
ILE HD11 H N N 175 
ILE HD12 H N N 176 
ILE HD13 H N N 177 
ILE HXT  H N N 178 
LEU N    N N N 179 
LEU CA   C N S 180 
LEU C    C N N 181 
LEU O    O N N 182 
LEU CB   C N N 183 
LEU CG   C N N 184 
LEU CD1  C N N 185 
LEU CD2  C N N 186 
LEU OXT  O N N 187 
LEU H    H N N 188 
LEU H2   H N N 189 
LEU HA   H N N 190 
LEU HB2  H N N 191 
LEU HB3  H N N 192 
LEU HG   H N N 193 
LEU HD11 H N N 194 
LEU HD12 H N N 195 
LEU HD13 H N N 196 
LEU HD21 H N N 197 
LEU HD22 H N N 198 
LEU HD23 H N N 199 
LEU HXT  H N N 200 
LYS N    N N N 201 
LYS CA   C N S 202 
LYS C    C N N 203 
LYS O    O N N 204 
LYS CB   C N N 205 
LYS CG   C N N 206 
LYS CD   C N N 207 
LYS CE   C N N 208 
LYS NZ   N N N 209 
LYS OXT  O N N 210 
LYS H    H N N 211 
LYS H2   H N N 212 
LYS HA   H N N 213 
LYS HB2  H N N 214 
LYS HB3  H N N 215 
LYS HG2  H N N 216 
LYS HG3  H N N 217 
LYS HD2  H N N 218 
LYS HD3  H N N 219 
LYS HE2  H N N 220 
LYS HE3  H N N 221 
LYS HZ1  H N N 222 
LYS HZ2  H N N 223 
LYS HZ3  H N N 224 
LYS HXT  H N N 225 
MET N    N N N 226 
MET CA   C N S 227 
MET C    C N N 228 
MET O    O N N 229 
MET CB   C N N 230 
MET CG   C N N 231 
MET SD   S N N 232 
MET CE   C N N 233 
MET OXT  O N N 234 
MET H    H N N 235 
MET H2   H N N 236 
MET HA   H N N 237 
MET HB2  H N N 238 
MET HB3  H N N 239 
MET HG2  H N N 240 
MET HG3  H N N 241 
MET HE1  H N N 242 
MET HE2  H N N 243 
MET HE3  H N N 244 
MET HXT  H N N 245 
NO3 N    N N N 246 
NO3 O1   O N N 247 
NO3 O2   O N N 248 
NO3 O3   O N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
EDO C1  O1   sing N N 70  
EDO C1  C2   sing N N 71  
EDO C1  H11  sing N N 72  
EDO C1  H12  sing N N 73  
EDO O1  HO1  sing N N 74  
EDO C2  O2   sing N N 75  
EDO C2  H21  sing N N 76  
EDO C2  H22  sing N N 77  
EDO O2  HO2  sing N N 78  
GLN N   CA   sing N N 79  
GLN N   H    sing N N 80  
GLN N   H2   sing N N 81  
GLN CA  C    sing N N 82  
GLN CA  CB   sing N N 83  
GLN CA  HA   sing N N 84  
GLN C   O    doub N N 85  
GLN C   OXT  sing N N 86  
GLN CB  CG   sing N N 87  
GLN CB  HB2  sing N N 88  
GLN CB  HB3  sing N N 89  
GLN CG  CD   sing N N 90  
GLN CG  HG2  sing N N 91  
GLN CG  HG3  sing N N 92  
GLN CD  OE1  doub N N 93  
GLN CD  NE2  sing N N 94  
GLN NE2 HE21 sing N N 95  
GLN NE2 HE22 sing N N 96  
GLN OXT HXT  sing N N 97  
GLU N   CA   sing N N 98  
GLU N   H    sing N N 99  
GLU N   H2   sing N N 100 
GLU CA  C    sing N N 101 
GLU CA  CB   sing N N 102 
GLU CA  HA   sing N N 103 
GLU C   O    doub N N 104 
GLU C   OXT  sing N N 105 
GLU CB  CG   sing N N 106 
GLU CB  HB2  sing N N 107 
GLU CB  HB3  sing N N 108 
GLU CG  CD   sing N N 109 
GLU CG  HG2  sing N N 110 
GLU CG  HG3  sing N N 111 
GLU CD  OE1  doub N N 112 
GLU CD  OE2  sing N N 113 
GLU OE2 HE2  sing N N 114 
GLU OXT HXT  sing N N 115 
GLY N   CA   sing N N 116 
GLY N   H    sing N N 117 
GLY N   H2   sing N N 118 
GLY CA  C    sing N N 119 
GLY CA  HA2  sing N N 120 
GLY CA  HA3  sing N N 121 
GLY C   O    doub N N 122 
GLY C   OXT  sing N N 123 
GLY OXT HXT  sing N N 124 
HIS N   CA   sing N N 125 
HIS N   H    sing N N 126 
HIS N   H2   sing N N 127 
HIS CA  C    sing N N 128 
HIS CA  CB   sing N N 129 
HIS CA  HA   sing N N 130 
HIS C   O    doub N N 131 
HIS C   OXT  sing N N 132 
HIS CB  CG   sing N N 133 
HIS CB  HB2  sing N N 134 
HIS CB  HB3  sing N N 135 
HIS CG  ND1  sing Y N 136 
HIS CG  CD2  doub Y N 137 
HIS ND1 CE1  doub Y N 138 
HIS ND1 HD1  sing N N 139 
HIS CD2 NE2  sing Y N 140 
HIS CD2 HD2  sing N N 141 
HIS CE1 NE2  sing Y N 142 
HIS CE1 HE1  sing N N 143 
HIS NE2 HE2  sing N N 144 
HIS OXT HXT  sing N N 145 
HOH O   H1   sing N N 146 
HOH O   H2   sing N N 147 
ILE N   CA   sing N N 148 
ILE N   H    sing N N 149 
ILE N   H2   sing N N 150 
ILE CA  C    sing N N 151 
ILE CA  CB   sing N N 152 
ILE CA  HA   sing N N 153 
ILE C   O    doub N N 154 
ILE C   OXT  sing N N 155 
ILE CB  CG1  sing N N 156 
ILE CB  CG2  sing N N 157 
ILE CB  HB   sing N N 158 
ILE CG1 CD1  sing N N 159 
ILE CG1 HG12 sing N N 160 
ILE CG1 HG13 sing N N 161 
ILE CG2 HG21 sing N N 162 
ILE CG2 HG22 sing N N 163 
ILE CG2 HG23 sing N N 164 
ILE CD1 HD11 sing N N 165 
ILE CD1 HD12 sing N N 166 
ILE CD1 HD13 sing N N 167 
ILE OXT HXT  sing N N 168 
LEU N   CA   sing N N 169 
LEU N   H    sing N N 170 
LEU N   H2   sing N N 171 
LEU CA  C    sing N N 172 
LEU CA  CB   sing N N 173 
LEU CA  HA   sing N N 174 
LEU C   O    doub N N 175 
LEU C   OXT  sing N N 176 
LEU CB  CG   sing N N 177 
LEU CB  HB2  sing N N 178 
LEU CB  HB3  sing N N 179 
LEU CG  CD1  sing N N 180 
LEU CG  CD2  sing N N 181 
LEU CG  HG   sing N N 182 
LEU CD1 HD11 sing N N 183 
LEU CD1 HD12 sing N N 184 
LEU CD1 HD13 sing N N 185 
LEU CD2 HD21 sing N N 186 
LEU CD2 HD22 sing N N 187 
LEU CD2 HD23 sing N N 188 
LEU OXT HXT  sing N N 189 
LYS N   CA   sing N N 190 
LYS N   H    sing N N 191 
LYS N   H2   sing N N 192 
LYS CA  C    sing N N 193 
LYS CA  CB   sing N N 194 
LYS CA  HA   sing N N 195 
LYS C   O    doub N N 196 
LYS C   OXT  sing N N 197 
LYS CB  CG   sing N N 198 
LYS CB  HB2  sing N N 199 
LYS CB  HB3  sing N N 200 
LYS CG  CD   sing N N 201 
LYS CG  HG2  sing N N 202 
LYS CG  HG3  sing N N 203 
LYS CD  CE   sing N N 204 
LYS CD  HD2  sing N N 205 
LYS CD  HD3  sing N N 206 
LYS CE  NZ   sing N N 207 
LYS CE  HE2  sing N N 208 
LYS CE  HE3  sing N N 209 
LYS NZ  HZ1  sing N N 210 
LYS NZ  HZ2  sing N N 211 
LYS NZ  HZ3  sing N N 212 
LYS OXT HXT  sing N N 213 
MET N   CA   sing N N 214 
MET N   H    sing N N 215 
MET N   H2   sing N N 216 
MET CA  C    sing N N 217 
MET CA  CB   sing N N 218 
MET CA  HA   sing N N 219 
MET C   O    doub N N 220 
MET C   OXT  sing N N 221 
MET CB  CG   sing N N 222 
MET CB  HB2  sing N N 223 
MET CB  HB3  sing N N 224 
MET CG  SD   sing N N 225 
MET CG  HG2  sing N N 226 
MET CG  HG3  sing N N 227 
MET SD  CE   sing N N 228 
MET CE  HE1  sing N N 229 
MET CE  HE2  sing N N 230 
MET CE  HE3  sing N N 231 
MET OXT HXT  sing N N 232 
NO3 N   O1   doub N N 233 
NO3 N   O2   sing N N 234 
NO3 N   O3   sing N N 235 
PHE N   CA   sing N N 236 
PHE N   H    sing N N 237 
PHE N   H2   sing N N 238 
PHE CA  C    sing N N 239 
PHE CA  CB   sing N N 240 
PHE CA  HA   sing N N 241 
PHE C   O    doub N N 242 
PHE C   OXT  sing N N 243 
PHE CB  CG   sing N N 244 
PHE CB  HB2  sing N N 245 
PHE CB  HB3  sing N N 246 
PHE CG  CD1  doub Y N 247 
PHE CG  CD2  sing Y N 248 
PHE CD1 CE1  sing Y N 249 
PHE CD1 HD1  sing N N 250 
PHE CD2 CE2  doub Y N 251 
PHE CD2 HD2  sing N N 252 
PHE CE1 CZ   doub Y N 253 
PHE CE1 HE1  sing N N 254 
PHE CE2 CZ   sing Y N 255 
PHE CE2 HE2  sing N N 256 
PHE CZ  HZ   sing N N 257 
PHE OXT HXT  sing N N 258 
PRO N   CA   sing N N 259 
PRO N   CD   sing N N 260 
PRO N   H    sing N N 261 
PRO CA  C    sing N N 262 
PRO CA  CB   sing N N 263 
PRO CA  HA   sing N N 264 
PRO C   O    doub N N 265 
PRO C   OXT  sing N N 266 
PRO CB  CG   sing N N 267 
PRO CB  HB2  sing N N 268 
PRO CB  HB3  sing N N 269 
PRO CG  CD   sing N N 270 
PRO CG  HG2  sing N N 271 
PRO CG  HG3  sing N N 272 
PRO CD  HD2  sing N N 273 
PRO CD  HD3  sing N N 274 
PRO OXT HXT  sing N N 275 
SER N   CA   sing N N 276 
SER N   H    sing N N 277 
SER N   H2   sing N N 278 
SER CA  C    sing N N 279 
SER CA  CB   sing N N 280 
SER CA  HA   sing N N 281 
SER C   O    doub N N 282 
SER C   OXT  sing N N 283 
SER CB  OG   sing N N 284 
SER CB  HB2  sing N N 285 
SER CB  HB3  sing N N 286 
SER OG  HG   sing N N 287 
SER OXT HXT  sing N N 288 
THR N   CA   sing N N 289 
THR N   H    sing N N 290 
THR N   H2   sing N N 291 
THR CA  C    sing N N 292 
THR CA  CB   sing N N 293 
THR CA  HA   sing N N 294 
THR C   O    doub N N 295 
THR C   OXT  sing N N 296 
THR CB  OG1  sing N N 297 
THR CB  CG2  sing N N 298 
THR CB  HB   sing N N 299 
THR OG1 HG1  sing N N 300 
THR CG2 HG21 sing N N 301 
THR CG2 HG22 sing N N 302 
THR CG2 HG23 sing N N 303 
THR OXT HXT  sing N N 304 
TRP N   CA   sing N N 305 
TRP N   H    sing N N 306 
TRP N   H2   sing N N 307 
TRP CA  C    sing N N 308 
TRP CA  CB   sing N N 309 
TRP CA  HA   sing N N 310 
TRP C   O    doub N N 311 
TRP C   OXT  sing N N 312 
TRP CB  CG   sing N N 313 
TRP CB  HB2  sing N N 314 
TRP CB  HB3  sing N N 315 
TRP CG  CD1  doub Y N 316 
TRP CG  CD2  sing Y N 317 
TRP CD1 NE1  sing Y N 318 
TRP CD1 HD1  sing N N 319 
TRP CD2 CE2  doub Y N 320 
TRP CD2 CE3  sing Y N 321 
TRP NE1 CE2  sing Y N 322 
TRP NE1 HE1  sing N N 323 
TRP CE2 CZ2  sing Y N 324 
TRP CE3 CZ3  doub Y N 325 
TRP CE3 HE3  sing N N 326 
TRP CZ2 CH2  doub Y N 327 
TRP CZ2 HZ2  sing N N 328 
TRP CZ3 CH2  sing Y N 329 
TRP CZ3 HZ3  sing N N 330 
TRP CH2 HH2  sing N N 331 
TRP OXT HXT  sing N N 332 
TYR N   CA   sing N N 333 
TYR N   H    sing N N 334 
TYR N   H2   sing N N 335 
TYR CA  C    sing N N 336 
TYR CA  CB   sing N N 337 
TYR CA  HA   sing N N 338 
TYR C   O    doub N N 339 
TYR C   OXT  sing N N 340 
TYR CB  CG   sing N N 341 
TYR CB  HB2  sing N N 342 
TYR CB  HB3  sing N N 343 
TYR CG  CD1  doub Y N 344 
TYR CG  CD2  sing Y N 345 
TYR CD1 CE1  sing Y N 346 
TYR CD1 HD1  sing N N 347 
TYR CD2 CE2  doub Y N 348 
TYR CD2 HD2  sing N N 349 
TYR CE1 CZ   doub Y N 350 
TYR CE1 HE1  sing N N 351 
TYR CE2 CZ   sing Y N 352 
TYR CE2 HE2  sing N N 353 
TYR CZ  OH   sing N N 354 
TYR OH  HH   sing N N 355 
TYR OXT HXT  sing N N 356 
VAL N   CA   sing N N 357 
VAL N   H    sing N N 358 
VAL N   H2   sing N N 359 
VAL CA  C    sing N N 360 
VAL CA  CB   sing N N 361 
VAL CA  HA   sing N N 362 
VAL C   O    doub N N 363 
VAL C   OXT  sing N N 364 
VAL CB  CG1  sing N N 365 
VAL CB  CG2  sing N N 366 
VAL CB  HB   sing N N 367 
VAL CG1 HG11 sing N N 368 
VAL CG1 HG12 sing N N 369 
VAL CG1 HG13 sing N N 370 
VAL CG2 HG21 sing N N 371 
VAL CG2 HG22 sing N N 372 
VAL CG2 HG23 sing N N 373 
VAL OXT HXT  sing N N 374 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R01AI155723 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   9MTU 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9MTV 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023208 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003846 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005488 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.019967 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASN A 1 2   ? -0.883  -8.123  21.167  1.00 70.49 ? 3   ASN A N   1 
ATOM   2    C CA  . ASN A 1 2   ? 0.351   -8.902  21.202  1.00 66.05 ? 3   ASN A CA  1 
ATOM   3    C C   . ASN A 1 2   ? 0.492   -9.690  22.505  1.00 66.52 ? 3   ASN A C   1 
ATOM   4    O O   . ASN A 1 2   ? 0.504   -9.113  23.591  1.00 65.87 ? 3   ASN A O   1 
ATOM   5    C CB  . ASN A 1 2   ? 1.559   -7.986  21.010  1.00 67.01 ? 3   ASN A CB  1 
ATOM   6    C CG  . ASN A 1 2   ? 1.994   -7.893  19.563  1.00 66.16 ? 3   ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 2   ? 1.307   -8.374  18.662  1.00 68.08 ? 3   ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 2   ? 3.146   -7.274  19.331  1.00 64.04 ? 3   ASN A ND2 1 
ATOM   9    N N   . THR A 1 3   ? 0.616   -11.016 22.378  1.00 67.12 ? 4   THR A N   1 
ATOM   10   C CA  . THR A 1 3   ? 0.680   -11.943 23.504  1.00 69.43 ? 4   THR A CA  1 
ATOM   11   C C   . THR A 1 3   ? 1.913   -11.675 24.364  1.00 72.20 ? 4   THR A C   1 
ATOM   12   O O   . THR A 1 3   ? 2.797   -10.905 23.956  1.00 68.11 ? 4   THR A O   1 
ATOM   13   C CB  . THR A 1 3   ? 0.690   -13.391 22.997  1.00 68.18 ? 4   THR A CB  1 
ATOM   14   O OG1 . THR A 1 3   ? 1.932   -13.663 22.336  1.00 64.74 ? 4   THR A OG1 1 
ATOM   15   C CG2 . THR A 1 3   ? -0.461  -13.629 22.027  1.00 70.54 ? 4   THR A CG2 1 
ATOM   16   N N   . PRO A 1 4   ? 2.004   -12.268 25.564  1.00 62.47 ? 5   PRO A N   1 
ATOM   17   C CA  . PRO A 1 4   ? 3.264   -12.169 26.322  1.00 58.50 ? 5   PRO A CA  1 
ATOM   18   C C   . PRO A 1 4   ? 4.467   -12.668 25.545  1.00 54.02 ? 5   PRO A C   1 
ATOM   19   O O   . PRO A 1 4   ? 5.553   -12.088 25.658  1.00 52.28 ? 5   PRO A O   1 
ATOM   20   C CB  . PRO A 1 4   ? 2.992   -13.033 27.563  1.00 61.78 ? 5   PRO A CB  1 
ATOM   21   C CG  . PRO A 1 4   ? 1.515   -12.976 27.739  1.00 62.30 ? 5   PRO A CG  1 
ATOM   22   C CD  . PRO A 1 4   ? 0.937   -12.915 26.352  1.00 64.14 ? 5   PRO A CD  1 
ATOM   23   N N   . LYS A 1 5   ? 4.299   -13.735 24.756  1.00 54.61 ? 6   LYS A N   1 
ATOM   24   C CA  . LYS A 1 5   ? 5.390   -14.229 23.919  1.00 51.79 ? 6   LYS A CA  1 
ATOM   25   C C   . LYS A 1 5   ? 5.786   -13.208 22.860  1.00 46.07 ? 6   LYS A C   1 
ATOM   26   O O   . LYS A 1 5   ? 6.979   -12.993 22.619  1.00 44.56 ? 6   LYS A O   1 
ATOM   27   C CB  . LYS A 1 5   ? 4.992   -15.548 23.256  1.00 46.47 ? 6   LYS A CB  1 
ATOM   28   C CG  . LYS A 1 5   ? 5.486   -16.772 23.974  1.00 49.14 ? 6   LYS A CG  1 
ATOM   29   C CD  . LYS A 1 5   ? 6.932   -17.068 23.625  1.00 48.13 ? 6   LYS A CD  1 
ATOM   30   C CE  . LYS A 1 5   ? 7.486   -18.123 24.554  1.00 50.54 ? 6   LYS A CE  1 
ATOM   31   N NZ  . LYS A 1 5   ? 6.549   -19.265 24.667  1.00 52.41 ? 6   LYS A NZ  1 
ATOM   32   N N   . ASP A 1 6   ? 4.800   -12.592 22.197  1.00 50.09 ? 7   ASP A N   1 
ATOM   33   C CA  . ASP A 1 6   ? 5.093   -11.562 21.202  1.00 48.66 ? 7   ASP A CA  1 
ATOM   34   C C   . ASP A 1 6   ? 6.052   -10.524 21.763  1.00 46.28 ? 7   ASP A C   1 
ATOM   35   O O   . ASP A 1 6   ? 7.065   -10.188 21.140  1.00 41.54 ? 7   ASP A O   1 
ATOM   36   C CB  . ASP A 1 6   ? 3.801   -10.879 20.742  1.00 54.50 ? 7   ASP A CB  1 
ATOM   37   C CG  . ASP A 1 6   ? 2.843   -11.828 20.039  1.00 58.79 ? 7   ASP A CG  1 
ATOM   38   O OD1 . ASP A 1 6   ? 3.302   -12.649 19.217  1.00 55.12 ? 7   ASP A OD1 1 
ATOM   39   O OD2 . ASP A 1 6   ? 1.622   -11.742 20.300  1.00 62.96 ? 7   ASP A OD2 1 
ATOM   40   N N   . GLN A 1 7   ? 5.746   -10.014 22.958  1.00 49.03 ? 8   GLN A N   1 
ATOM   41   C CA  . GLN A 1 7   ? 6.554   -8.955  23.551  1.00 45.30 ? 8   GLN A CA  1 
ATOM   42   C C   . GLN A 1 7   ? 7.949   -9.452  23.894  1.00 37.60 ? 8   GLN A C   1 
ATOM   43   O O   . GLN A 1 7   ? 8.943   -8.783  23.591  1.00 36.85 ? 8   GLN A O   1 
ATOM   44   C CB  . GLN A 1 7   ? 5.865   -8.409  24.803  1.00 47.51 ? 8   GLN A CB  1 
ATOM   45   C CG  . GLN A 1 7   ? 4.408   -8.047  24.613  1.00 53.01 ? 8   GLN A CG  1 
ATOM   46   C CD  . GLN A 1 7   ? 3.800   -7.445  25.869  1.00 59.54 ? 8   GLN A CD  1 
ATOM   47   O OE1 . GLN A 1 7   ? 2.610   -7.135  25.906  1.00 62.19 ? 8   GLN A OE1 1 
ATOM   48   N NE2 . GLN A 1 7   ? 4.620   -7.278  26.907  1.00 57.06 ? 8   GLN A NE2 1 
ATOM   49   N N   . GLU A 1 8   ? 8.036   -10.618 24.549  1.00 36.87 ? 9   GLU A N   1 
ATOM   50   C CA  . GLU A 1 8   ? 9.327   -11.150 24.979  1.00 42.31 ? 9   GLU A CA  1 
ATOM   51   C C   . GLU A 1 8   ? 10.254  -11.364 23.786  1.00 38.78 ? 9   GLU A C   1 
ATOM   52   O O   . GLU A 1 8   ? 11.432  -10.984 23.823  1.00 34.88 ? 9   GLU A O   1 
ATOM   53   C CB  . GLU A 1 8   ? 9.124   -12.462 25.750  1.00 41.61 ? 9   GLU A CB  1 
ATOM   54   C CG  . GLU A 1 8   ? 10.418  -13.095 26.298  1.00 48.52 ? 9   GLU A CG  1 
ATOM   55   C CD  . GLU A 1 8   ? 10.346  -14.634 26.459  1.00 60.47 ? 9   GLU A CD  1 
ATOM   56   O OE1 . GLU A 1 8   ? 9.275   -15.237 26.207  1.00 60.11 ? 9   GLU A OE1 1 
ATOM   57   O OE2 . GLU A 1 8   ? 11.372  -15.246 26.839  1.00 56.71 ? 9   GLU A OE2 1 
ATOM   58   N N   . ILE A 1 9   ? 9.730   -11.964 22.712  1.00 35.77 ? 10  ILE A N   1 
ATOM   59   C CA  . ILE A 1 9   ? 10.554  -12.298 21.554  1.00 36.68 ? 10  ILE A CA  1 
ATOM   60   C C   . ILE A 1 9   ? 10.980  -11.038 20.808  1.00 34.85 ? 10  ILE A C   1 
ATOM   61   O O   . ILE A 1 9   ? 12.136  -10.915 20.380  1.00 32.97 ? 10  ILE A O   1 
ATOM   62   C CB  . ILE A 1 9   ? 9.800   -13.285 20.642  1.00 34.39 ? 10  ILE A CB  1 
ATOM   63   C CG1 . ILE A 1 9   ? 9.660   -14.634 21.351  1.00 34.74 ? 10  ILE A CG1 1 
ATOM   64   C CG2 . ILE A 1 9   ? 10.509  -13.433 19.309  1.00 33.61 ? 10  ILE A CG2 1 
ATOM   65   C CD1 . ILE A 1 9   ? 8.984   -15.683 20.514  1.00 39.68 ? 10  ILE A CD1 1 
ATOM   66   N N   . LYS A 1 10  ? 10.063  -10.083 20.637  1.00 34.34 ? 11  LYS A N   1 
ATOM   67   C CA  . LYS A 1 10  ? 10.454  -8.795  20.072  1.00 37.03 ? 11  LYS A CA  1 
ATOM   68   C C   . LYS A 1 10  ? 11.617  -8.197  20.853  1.00 36.13 ? 11  LYS A C   1 
ATOM   69   O O   . LYS A 1 10  ? 12.616  -7.756  20.273  1.00 34.70 ? 11  LYS A O   1 
ATOM   70   C CB  . LYS A 1 10  ? 9.269   -7.826  20.067  1.00 37.97 ? 11  LYS A CB  1 
ATOM   71   C CG  . LYS A 1 10  ? 9.653   -6.419  19.600  1.00 43.39 ? 11  LYS A CG  1 
ATOM   72   C CD  . LYS A 1 10  ? 8.603   -5.377  19.969  1.00 44.94 ? 11  LYS A CD  1 
ATOM   73   C CE  . LYS A 1 10  ? 9.205   -3.979  20.016  1.00 46.86 ? 11  LYS A CE  1 
ATOM   74   N NZ  . LYS A 1 10  ? 9.938   -3.664  18.761  1.00 48.08 ? 11  LYS A NZ  1 
ATOM   75   N N   . LYS A 1 11  ? 11.511  -8.199  22.181  1.00 37.55 ? 12  LYS A N   1 
ATOM   76   C CA  . LYS A 1 11  ? 12.558  -7.601  23.004  1.00 35.91 ? 12  LYS A CA  1 
ATOM   77   C C   . LYS A 1 11  ? 13.897  -8.305  22.795  1.00 36.11 ? 12  LYS A C   1 
ATOM   78   O O   . LYS A 1 11  ? 14.932  -7.654  22.622  1.00 34.62 ? 12  LYS A O   1 
ATOM   79   C CB  . LYS A 1 11  ? 12.146  -7.635  24.473  1.00 34.64 ? 12  LYS A CB  1 
ATOM   80   C CG  . LYS A 1 11  ? 12.932  -6.676  25.323  1.00 43.60 ? 12  LYS A CG  1 
ATOM   81   C CD  . LYS A 1 11  ? 12.564  -6.779  26.795  1.00 49.38 ? 12  LYS A CD  1 
ATOM   82   C CE  . LYS A 1 11  ? 13.016  -5.533  27.546  1.00 52.44 ? 12  LYS A CE  1 
ATOM   83   N NZ  . LYS A 1 11  ? 13.525  -5.849  28.911  1.00 57.68 ? 12  LYS A NZ  1 
ATOM   84   N N   . LEU A 1 12  ? 13.895  -9.641  22.788  1.00 34.01 ? 13  LEU A N   1 
ATOM   85   C CA  . LEU A 1 12  ? 15.139  -10.378 22.574  1.00 33.40 ? 13  LEU A CA  1 
ATOM   86   C C   . LEU A 1 12  ? 15.748  -10.072 21.212  1.00 32.15 ? 13  LEU A C   1 
ATOM   87   O O   . LEU A 1 12  ? 16.972  -9.933  21.088  1.00 27.04 ? 13  LEU A O   1 
ATOM   88   C CB  . LEU A 1 12  ? 14.893  -11.879 22.709  1.00 35.73 ? 13  LEU A CB  1 
ATOM   89   C CG  . LEU A 1 12  ? 14.521  -12.378 24.097  1.00 36.08 ? 13  LEU A CG  1 
ATOM   90   C CD1 . LEU A 1 12  ? 14.128  -13.852 24.036  1.00 34.60 ? 13  LEU A CD1 1 
ATOM   91   C CD2 . LEU A 1 12  ? 15.690  -12.157 25.040  1.00 37.63 ? 13  LEU A CD2 1 
ATOM   92   N N   . VAL A 1 13  ? 14.917  -9.984  20.172  1.00 30.23 ? 14  VAL A N   1 
ATOM   93   C CA  . VAL A 1 13  ? 15.449  -9.696  18.844  1.00 30.27 ? 14  VAL A CA  1 
ATOM   94   C C   . VAL A 1 13  ? 15.938  -8.253  18.765  1.00 34.58 ? 14  VAL A C   1 
ATOM   95   O O   . VAL A 1 13  ? 16.999  -7.977  18.188  1.00 29.87 ? 14  VAL A O   1 
ATOM   96   C CB  . VAL A 1 13  ? 14.401  -10.028 17.761  1.00 29.36 ? 14  VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 13  ? 14.902  -9.606  16.388  1.00 31.00 ? 14  VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 13  ? 14.114  -11.538 17.757  1.00 30.07 ? 14  VAL A CG2 1 
ATOM   99   N N   . ASP A 1 14  ? 15.200  -7.314  19.376  1.00 31.81 ? 15  ASP A N   1 
ATOM   100  C CA  . ASP A 1 14  ? 15.672  -5.927  19.420  1.00 34.94 ? 15  ASP A CA  1 
ATOM   101  C C   . ASP A 1 14  ? 17.003  -5.823  20.148  1.00 34.83 ? 15  ASP A C   1 
ATOM   102  O O   . ASP A 1 14  ? 17.845  -4.992  19.791  1.00 38.44 ? 15  ASP A O   1 
ATOM   103  C CB  . ASP A 1 14  ? 14.650  -5.014  20.108  1.00 33.80 ? 15  ASP A CB  1 
ATOM   104  C CG  . ASP A 1 14  ? 13.432  -4.716  19.248  1.00 37.71 ? 15  ASP A CG  1 
ATOM   105  O OD1 . ASP A 1 14  ? 13.449  -4.989  18.031  1.00 38.98 ? 15  ASP A OD1 1 
ATOM   106  O OD2 . ASP A 1 14  ? 12.437  -4.204  19.805  1.00 42.86 ? 15  ASP A OD2 1 
ATOM   107  N N   . GLN A 1 15  ? 17.207  -6.659  21.171  1.00 33.43 ? 16  GLN A N   1 
ATOM   108  C CA  . GLN A 1 15  ? 18.412  -6.575  21.988  1.00 34.92 ? 16  GLN A CA  1 
ATOM   109  C C   . GLN A 1 15  ? 19.632  -7.160  21.296  1.00 32.17 ? 16  GLN A C   1 
ATOM   110  O O   . GLN A 1 15  ? 20.754  -6.730  21.575  1.00 34.78 ? 16  GLN A O   1 
ATOM   111  C CB  . GLN A 1 15  ? 18.206  -7.305  23.312  1.00 36.57 ? 16  GLN A CB  1 
ATOM   112  C CG  . GLN A 1 15  ? 17.326  -6.582  24.307  1.00 41.82 ? 16  GLN A CG  1 
ATOM   113  C CD  . GLN A 1 15  ? 16.998  -7.456  25.508  1.00 47.10 ? 16  GLN A CD  1 
ATOM   114  O OE1 . GLN A 1 15  ? 17.673  -8.457  25.773  1.00 48.28 ? 16  GLN A OE1 1 
ATOM   115  N NE2 . GLN A 1 15  ? 15.961  -7.076  26.246  1.00 52.97 ? 16  GLN A NE2 1 
ATOM   116  N N   . ASN A 1 16  ? 19.452  -8.146  20.422  1.00 31.13 ? 17  ASN A N   1 
ATOM   117  C CA  . ASN A 1 16  ? 20.581  -8.901  19.903  1.00 30.53 ? 17  ASN A CA  1 
ATOM   118  C C   . ASN A 1 16  ? 20.813  -8.752  18.408  1.00 30.38 ? 17  ASN A C   1 
ATOM   119  O O   . ASN A 1 16  ? 21.968  -8.841  17.971  1.00 31.40 ? 17  ASN A O   1 
ATOM   120  C CB  . ASN A 1 16  ? 20.410  -10.387 20.237  1.00 32.54 ? 17  ASN A CB  1 
ATOM   121  C CG  . ASN A 1 16  ? 20.500  -10.642 21.710  1.00 34.40 ? 17  ASN A CG  1 
ATOM   122  O OD1 . ASN A 1 16  ? 21.591  -10.638 22.278  1.00 31.77 ? 17  ASN A OD1 1 
ATOM   123  N ND2 . ASN A 1 16  ? 19.356  -10.840 22.350  1.00 32.79 ? 17  ASN A ND2 1 
ATOM   124  N N   . PHE A 1 17  ? 19.768  -8.527  17.615  1.00 27.89 ? 18  PHE A N   1 
ATOM   125  C CA  . PHE A 1 17  ? 19.938  -8.355  16.174  1.00 28.40 ? 18  PHE A CA  1 
ATOM   126  C C   . PHE A 1 17  ? 19.895  -6.899  15.739  1.00 30.77 ? 18  PHE A C   1 
ATOM   127  O O   . PHE A 1 17  ? 20.697  -6.483  14.898  1.00 30.52 ? 18  PHE A O   1 
ATOM   128  C CB  . PHE A 1 17  ? 18.860  -9.130  15.411  1.00 28.63 ? 18  PHE A CB  1 
ATOM   129  C CG  . PHE A 1 17  ? 19.088  -10.606 15.386  1.00 22.19 ? 18  PHE A CG  1 
ATOM   130  C CD1 . PHE A 1 17  ? 18.633  -11.414 16.417  1.00 24.76 ? 18  PHE A CD1 1 
ATOM   131  C CD2 . PHE A 1 17  ? 19.776  -11.192 14.335  1.00 28.07 ? 18  PHE A CD2 1 
ATOM   132  C CE1 . PHE A 1 17  ? 18.846  -12.800 16.384  1.00 24.74 ? 18  PHE A CE1 1 
ATOM   133  C CE2 . PHE A 1 17  ? 19.984  -12.568 14.294  1.00 24.32 ? 18  PHE A CE2 1 
ATOM   134  C CZ  . PHE A 1 17  ? 19.531  -13.370 15.323  1.00 25.08 ? 18  PHE A CZ  1 
ATOM   135  N N   . LYS A 1 18  ? 18.961  -6.127  16.274  1.00 30.80 ? 19  LYS A N   1 
ATOM   136  C CA  . LYS A 1 18  ? 18.813  -4.737  15.851  1.00 33.39 ? 19  LYS A CA  1 
ATOM   137  C C   . LYS A 1 18  ? 20.113  -3.934  15.903  1.00 35.32 ? 19  LYS A C   1 
ATOM   138  O O   . LYS A 1 18  ? 20.367  -3.179  14.948  1.00 34.50 ? 19  LYS A O   1 
ATOM   139  C CB  . LYS A 1 18  ? 17.717  -4.078  16.696  1.00 31.71 ? 19  LYS A CB  1 
ATOM   140  C CG  . LYS A 1 18  ? 17.321  -2.701  16.257  1.00 35.93 ? 19  LYS A CG  1 
ATOM   141  C CD  . LYS A 1 18  ? 16.338  -2.140  17.264  1.00 36.06 ? 19  LYS A CD  1 
ATOM   142  C CE  . LYS A 1 18  ? 16.025  -0.705  16.981  1.00 38.47 ? 19  LYS A CE  1 
ATOM   143  N NZ  . LYS A 1 18  ? 15.495  -0.050  18.207  1.00 41.84 ? 19  LYS A NZ  1 
ATOM   144  N N   . PRO A 1 19  ? 20.965  -4.040  16.938  1.00 33.83 ? 20  PRO A N   1 
ATOM   145  C CA  . PRO A 1 19  ? 22.223  -3.266  16.930  1.00 33.37 ? 20  PRO A CA  1 
ATOM   146  C C   . PRO A 1 19  ? 23.146  -3.571  15.755  1.00 35.19 ? 20  PRO A C   1 
ATOM   147  O O   . PRO A 1 19  ? 23.957  -2.708  15.384  1.00 35.68 ? 20  PRO A O   1 
ATOM   148  C CB  . PRO A 1 19  ? 22.877  -3.651  18.266  1.00 34.98 ? 20  PRO A CB  1 
ATOM   149  C CG  . PRO A 1 19  ? 21.747  -4.042  19.139  1.00 33.38 ? 20  PRO A CG  1 
ATOM   150  C CD  . PRO A 1 19  ? 20.757  -4.714  18.234  1.00 34.44 ? 20  PRO A CD  1 
ATOM   151  N N   . LEU A 1 20  ? 23.055  -4.765  15.157  1.00 32.13 ? 21  LEU A N   1 
ATOM   152  C CA  . LEU A 1 20  ? 23.892  -5.084  13.999  1.00 34.77 ? 21  LEU A CA  1 
ATOM   153  C C   . LEU A 1 20  ? 23.664  -4.127  12.831  1.00 34.49 ? 21  LEU A C   1 
ATOM   154  O O   . LEU A 1 20  ? 24.567  -3.934  12.008  1.00 31.75 ? 21  LEU A O   1 
ATOM   155  C CB  . LEU A 1 20  ? 23.634  -6.522  13.549  1.00 31.04 ? 21  LEU A CB  1 
ATOM   156  C CG  . LEU A 1 20  ? 23.968  -7.564  14.609  1.00 31.04 ? 21  LEU A CG  1 
ATOM   157  C CD1 . LEU A 1 20  ? 23.600  -8.956  14.092  1.00 26.53 ? 21  LEU A CD1 1 
ATOM   158  C CD2 . LEU A 1 20  ? 25.441  -7.480  14.979  1.00 32.87 ? 21  LEU A CD2 1 
ATOM   159  N N   . LEU A 1 21  ? 22.472  -3.528  12.733  1.00 34.69 ? 22  LEU A N   1 
ATOM   160  C CA  . LEU A 1 21  ? 22.174  -2.647  11.605  1.00 36.69 ? 22  LEU A CA  1 
ATOM   161  C C   . LEU A 1 21  ? 23.099  -1.435  11.579  1.00 35.61 ? 22  LEU A C   1 
ATOM   162  O O   . LEU A 1 21  ? 23.682  -1.113  10.538  1.00 32.18 ? 22  LEU A O   1 
ATOM   163  C CB  . LEU A 1 21  ? 20.719  -2.187  11.656  1.00 31.12 ? 22  LEU A CB  1 
ATOM   164  C CG  . LEU A 1 21  ? 19.646  -3.238  11.454  1.00 40.22 ? 22  LEU A CG  1 
ATOM   165  C CD1 . LEU A 1 21  ? 18.301  -2.578  11.680  1.00 40.00 ? 22  LEU A CD1 1 
ATOM   166  C CD2 . LEU A 1 21  ? 19.744  -3.833  10.058  1.00 34.83 ? 22  LEU A CD2 1 
ATOM   167  N N   . GLU A 1 22  ? 23.220  -0.728  12.707  1.00 36.20 ? 23  GLU A N   1 
ATOM   168  C CA  . GLU A 1 22  ? 24.123  0.417   12.750  1.00 38.53 ? 23  GLU A CA  1 
ATOM   169  C C   . GLU A 1 22  ? 25.576  -0.025  12.792  1.00 39.75 ? 23  GLU A C   1 
ATOM   170  O O   . GLU A 1 22  ? 26.445  0.655   12.239  1.00 39.65 ? 23  GLU A O   1 
ATOM   171  C CB  . GLU A 1 22  ? 23.815  1.299   13.959  1.00 43.77 ? 23  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 22  ? 24.561  2.626   13.953  1.00 54.39 ? 23  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 22  ? 24.378  3.410   15.241  1.00 65.04 ? 23  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 22  ? 25.265  4.228   15.575  1.00 68.04 ? 23  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 22  ? 23.348  3.206   15.920  1.00 69.23 ? 23  GLU A OE2 1 
ATOM   176  N N   . LYS A 1 23  ? 25.856  -1.164  13.433  1.00 39.47 ? 24  LYS A N   1 
ATOM   177  C CA  . LYS A 1 23  ? 27.240  -1.599  13.581  1.00 37.24 ? 24  LYS A CA  1 
ATOM   178  C C   . LYS A 1 23  ? 27.868  -1.898  12.231  1.00 37.42 ? 24  LYS A C   1 
ATOM   179  O O   . LYS A 1 23  ? 29.051  -1.617  12.016  1.00 38.80 ? 24  LYS A O   1 
ATOM   180  C CB  . LYS A 1 23  ? 27.325  -2.825  14.490  1.00 36.63 ? 24  LYS A CB  1 
ATOM   181  C CG  . LYS A 1 23  ? 28.749  -3.161  14.898  1.00 40.44 ? 24  LYS A CG  1 
ATOM   182  C CD  . LYS A 1 23  ? 28.833  -4.448  15.725  1.00 45.28 ? 24  LYS A CD  1 
ATOM   183  C CE  . LYS A 1 23  ? 30.280  -4.755  16.105  1.00 44.13 ? 24  LYS A CE  1 
ATOM   184  N NZ  . LYS A 1 23  ? 30.412  -5.951  16.964  1.00 41.91 ? 24  LYS A NZ  1 
ATOM   185  N N   . TYR A 1 24  ? 27.091  -2.449  11.299  1.00 37.89 ? 25  TYR A N   1 
ATOM   186  C CA  . TYR A 1 24  ? 27.631  -2.848  10.005  1.00 36.00 ? 25  TYR A CA  1 
ATOM   187  C C   . TYR A 1 24  ? 26.999  -2.112  8.832   1.00 36.04 ? 25  TYR A C   1 
ATOM   188  O O   . TYR A 1 24  ? 27.196  -2.526  7.682   1.00 37.39 ? 25  TYR A O   1 
ATOM   189  C CB  . TYR A 1 24  ? 27.490  -4.360  9.824   1.00 37.29 ? 25  TYR A CB  1 
ATOM   190  C CG  . TYR A 1 24  ? 28.365  -5.125  10.795  1.00 39.61 ? 25  TYR A CG  1 
ATOM   191  C CD1 . TYR A 1 24  ? 29.740  -5.195  10.608  1.00 37.51 ? 25  TYR A CD1 1 
ATOM   192  C CD2 . TYR A 1 24  ? 27.822  -5.744  11.910  1.00 35.56 ? 25  TYR A CD2 1 
ATOM   193  C CE1 . TYR A 1 24  ? 30.549  -5.869  11.493  1.00 40.83 ? 25  TYR A CE1 1 
ATOM   194  C CE2 . TYR A 1 24  ? 28.620  -6.425  12.804  1.00 40.20 ? 25  TYR A CE2 1 
ATOM   195  C CZ  . TYR A 1 24  ? 29.983  -6.490  12.588  1.00 41.27 ? 25  TYR A CZ  1 
ATOM   196  O OH  . TYR A 1 24  ? 30.781  -7.168  13.469  1.00 40.79 ? 25  TYR A OH  1 
ATOM   197  N N   . ASP A 1 25  ? 26.262  -1.031  9.094   1.00 37.87 ? 26  ASP A N   1 
ATOM   198  C CA  . ASP A 1 25  ? 25.612  -0.216  8.066   1.00 35.63 ? 26  ASP A CA  1 
ATOM   199  C C   . ASP A 1 25  ? 24.783  -1.066  7.102   1.00 33.26 ? 26  ASP A C   1 
ATOM   200  O O   . ASP A 1 25  ? 24.896  -0.952  5.877   1.00 31.92 ? 26  ASP A O   1 
ATOM   201  C CB  . ASP A 1 25  ? 26.639  0.628   7.309   1.00 34.71 ? 26  ASP A CB  1 
ATOM   202  C CG  . ASP A 1 25  ? 25.999  1.748   6.525   1.00 44.17 ? 26  ASP A CG  1 
ATOM   203  O OD1 . ASP A 1 25  ? 24.843  2.112   6.845   1.00 43.83 ? 26  ASP A OD1 1 
ATOM   204  O OD2 . ASP A 1 25  ? 26.650  2.260   5.588   1.00 43.73 ? 26  ASP A OD2 1 
ATOM   205  N N   . VAL A 1 26  ? 23.914  -1.898  7.671   1.00 31.27 ? 27  VAL A N   1 
ATOM   206  C CA  . VAL A 1 26  ? 23.055  -2.793  6.903   1.00 32.27 ? 27  VAL A CA  1 
ATOM   207  C C   . VAL A 1 26  ? 21.730  -2.073  6.646   1.00 28.37 ? 27  VAL A C   1 
ATOM   208  O O   . VAL A 1 26  ? 21.083  -1.648  7.612   1.00 29.89 ? 27  VAL A O   1 
ATOM   209  C CB  . VAL A 1 26  ? 22.812  -4.108  7.653   1.00 31.50 ? 27  VAL A CB  1 
ATOM   210  C CG1 . VAL A 1 26  ? 21.803  -4.947  6.909   1.00 27.93 ? 27  VAL A CG1 1 
ATOM   211  C CG2 . VAL A 1 26  ? 24.125  -4.866  7.855   1.00 35.36 ? 27  VAL A CG2 1 
ATOM   212  N N   . PRO A 1 27  ? 21.295  -1.922  5.389   1.00 31.64 ? 28  PRO A N   1 
ATOM   213  C CA  . PRO A 1 27  ? 20.038  -1.182  5.148   1.00 29.00 ? 28  PRO A CA  1 
ATOM   214  C C   . PRO A 1 27  ? 18.795  -1.854  5.708   1.00 27.06 ? 28  PRO A C   1 
ATOM   215  O O   . PRO A 1 27  ? 17.928  -1.157  6.248   1.00 27.22 ? 28  PRO A O   1 
ATOM   216  C CB  . PRO A 1 27  ? 19.971  -1.078  3.614   1.00 28.75 ? 28  PRO A CB  1 
ATOM   217  C CG  . PRO A 1 27  ? 21.380  -1.273  3.147   1.00 32.15 ? 28  PRO A CG  1 
ATOM   218  C CD  . PRO A 1 27  ? 22.015  -2.210  4.135   1.00 31.59 ? 28  PRO A CD  1 
ATOM   219  N N   . GLY A 1 28  ? 18.659  -3.173  5.570   1.00 28.04 ? 29  GLY A N   1 
ATOM   220  C CA  . GLY A 1 28  ? 17.424  -3.843  5.948   1.00 26.75 ? 29  GLY A CA  1 
ATOM   221  C C   . GLY A 1 28  ? 17.647  -5.238  6.498   1.00 24.58 ? 29  GLY A C   1 
ATOM   222  O O   . GLY A 1 28  ? 18.618  -5.924  6.151   1.00 24.49 ? 29  GLY A O   1 
ATOM   223  N N   . MET A 1 29  ? 16.712  -5.673  7.338   1.00 21.37 ? 30  MET A N   1 
ATOM   224  C CA  . MET A 1 29  ? 16.825  -6.973  7.982   1.00 22.58 ? 30  MET A CA  1 
ATOM   225  C C   . MET A 1 29  ? 15.442  -7.521  8.312   1.00 22.50 ? 30  MET A C   1 
ATOM   226  O O   . MET A 1 29  ? 14.545  -6.774  8.711   1.00 23.79 ? 30  MET A O   1 
ATOM   227  C CB  . MET A 1 29  ? 17.675  -6.871  9.253   1.00 23.72 ? 30  MET A CB  1 
ATOM   228  C CG  . MET A 1 29  ? 17.793  -8.176  10.040  1.00 25.73 ? 30  MET A CG  1 
ATOM   229  S SD  . MET A 1 29  ? 18.588  -7.944  11.642  1.00 32.48 ? 30  MET A SD  1 
ATOM   230  C CE  . MET A 1 29  ? 20.306  -7.798  11.215  1.00 29.62 ? 30  MET A CE  1 
ATOM   231  N N   . ALA A 1 30  ? 15.284  -8.837  8.161   1.00 24.89 ? 31  ALA A N   1 
ATOM   232  C CA  . ALA A 1 30  ? 14.100  -9.542  8.625   1.00 22.57 ? 31  ALA A CA  1 
ATOM   233  C C   . ALA A 1 30  ? 14.564  -10.676 9.530   1.00 23.62 ? 31  ALA A C   1 
ATOM   234  O O   . ALA A 1 30  ? 15.437  -11.461 9.139   1.00 23.41 ? 31  ALA A O   1 
ATOM   235  C CB  . ALA A 1 30  ? 13.265  -10.087 7.450   1.00 23.66 ? 31  ALA A CB  1 
ATOM   236  N N   . VAL A 1 31  ? 14.020  -10.740 10.746  1.00 20.32 ? 32  VAL A N   1 
ATOM   237  C CA  . VAL A 1 31  ? 14.351  -11.809 11.689  1.00 23.64 ? 32  VAL A CA  1 
ATOM   238  C C   . VAL A 1 31  ? 13.066  -12.456 12.175  1.00 20.82 ? 32  VAL A C   1 
ATOM   239  O O   . VAL A 1 31  ? 12.157  -11.762 12.634  1.00 22.33 ? 32  VAL A O   1 
ATOM   240  C CB  . VAL A 1 31  ? 15.173  -11.293 12.887  1.00 25.19 ? 32  VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 31  ? 15.506  -12.457 13.847  1.00 25.01 ? 32  VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 31  ? 16.446  -10.661 12.406  1.00 24.10 ? 32  VAL A CG2 1 
ATOM   243  N N   . GLY A 1 32  ? 13.000  -13.786 12.123  1.00 21.68 ? 33  GLY A N   1 
ATOM   244  C CA  . GLY A 1 32  ? 11.811  -14.492 12.549  1.00 22.01 ? 33  GLY A CA  1 
ATOM   245  C C   . GLY A 1 32  ? 12.125  -15.672 13.447  1.00 22.79 ? 33  GLY A C   1 
ATOM   246  O O   . GLY A 1 32  ? 13.193  -16.274 13.373  1.00 20.90 ? 33  GLY A O   1 
ATOM   247  N N   . VAL A 1 33  ? 11.173  -15.982 14.307  1.00 21.31 ? 34  VAL A N   1 
ATOM   248  C CA  . VAL A 1 33  ? 11.229  -17.137 15.190  1.00 23.33 ? 34  VAL A CA  1 
ATOM   249  C C   . VAL A 1 33  ? 9.959   -17.940 14.982  1.00 25.01 ? 34  VAL A C   1 
ATOM   250  O O   . VAL A 1 33  ? 8.864   -17.373 14.888  1.00 26.21 ? 34  VAL A O   1 
ATOM   251  C CB  . VAL A 1 33  ? 11.381  -16.700 16.661  1.00 26.22 ? 34  VAL A CB  1 
ATOM   252  C CG1 . VAL A 1 33  ? 11.033  -17.841 17.614  1.00 24.72 ? 34  VAL A CG1 1 
ATOM   253  C CG2 . VAL A 1 33  ? 12.795  -16.181 16.900  1.00 25.07 ? 34  VAL A CG2 1 
ATOM   254  N N   . ILE A 1 34  ? 10.103  -19.258 14.867  1.00 22.24 ? 35  ILE A N   1 
ATOM   255  C CA  . ILE A 1 34  ? 8.967   -20.167 14.828  1.00 24.06 ? 35  ILE A CA  1 
ATOM   256  C C   . ILE A 1 34  ? 9.062   -21.036 16.074  1.00 26.07 ? 35  ILE A C   1 
ATOM   257  O O   . ILE A 1 34  ? 10.145  -21.530 16.407  1.00 24.46 ? 35  ILE A O   1 
ATOM   258  C CB  . ILE A 1 34  ? 8.948   -21.009 13.529  1.00 24.07 ? 35  ILE A CB  1 
ATOM   259  C CG1 . ILE A 1 34  ? 7.818   -22.052 13.535  1.00 29.81 ? 35  ILE A CG1 1 
ATOM   260  C CG2 . ILE A 1 34  ? 10.316  -21.643 13.248  1.00 21.50 ? 35  ILE A CG2 1 
ATOM   261  C CD1 . ILE A 1 34  ? 6.526   -21.584 12.874  1.00 33.68 ? 35  ILE A CD1 1 
ATOM   262  N N   . GLN A 1 35  ? 7.960   -21.146 16.808  1.00 28.07 ? 36  GLN A N   1 
ATOM   263  C CA  . GLN A 1 35  ? 7.932   -21.964 18.021  1.00 27.87 ? 36  GLN A CA  1 
ATOM   264  C C   . GLN A 1 35  ? 6.543   -22.548 18.182  1.00 31.86 ? 36  GLN A C   1 
ATOM   265  O O   . GLN A 1 35  ? 5.565   -21.798 18.223  1.00 28.47 ? 36  GLN A O   1 
ATOM   266  C CB  . GLN A 1 35  ? 8.306   -21.146 19.262  1.00 31.34 ? 36  GLN A CB  1 
ATOM   267  C CG  . GLN A 1 35  ? 8.250   -21.963 20.553  1.00 33.95 ? 36  GLN A CG  1 
ATOM   268  C CD  . GLN A 1 35  ? 8.342   -21.124 21.827  1.00 41.13 ? 36  GLN A CD  1 
ATOM   269  O OE1 . GLN A 1 35  ? 7.714   -20.070 21.944  1.00 44.39 ? 36  GLN A OE1 1 
ATOM   270  N NE2 . GLN A 1 35  ? 9.112   -21.605 22.792  1.00 43.09 ? 36  GLN A NE2 1 
ATOM   271  N N   . ASN A 1 36  ? 6.458   -23.876 18.285  1.00 30.12 ? 37  ASN A N   1 
ATOM   272  C CA  . ASN A 1 36  ? 5.189   -24.558 18.518  1.00 34.68 ? 37  ASN A CA  1 
ATOM   273  C C   . ASN A 1 36  ? 4.118   -24.087 17.537  1.00 34.73 ? 37  ASN A C   1 
ATOM   274  O O   . ASN A 1 36  ? 2.998   -23.754 17.921  1.00 35.82 ? 37  ASN A O   1 
ATOM   275  C CB  . ASN A 1 36  ? 4.721   -24.361 19.962  1.00 39.05 ? 37  ASN A CB  1 
ATOM   276  C CG  . ASN A 1 36  ? 5.689   -24.941 20.972  1.00 40.45 ? 37  ASN A CG  1 
ATOM   277  O OD1 . ASN A 1 36  ? 6.145   -24.249 21.886  1.00 46.20 ? 37  ASN A OD1 1 
ATOM   278  N ND2 . ASN A 1 36  ? 6.007   -26.215 20.815  1.00 39.43 ? 37  ASN A ND2 1 
ATOM   279  N N   . ASN A 1 37  ? 4.485   -24.036 16.257  1.00 34.28 ? 38  ASN A N   1 
ATOM   280  C CA  . ASN A 1 37  ? 3.603   -23.674 15.145  1.00 38.13 ? 38  ASN A CA  1 
ATOM   281  C C   . ASN A 1 37  ? 3.180   -22.202 15.143  1.00 36.99 ? 38  ASN A C   1 
ATOM   282  O O   . ASN A 1 37  ? 2.243   -21.846 14.413  1.00 38.99 ? 38  ASN A O   1 
ATOM   283  C CB  . ASN A 1 37  ? 2.332   -24.538 15.098  1.00 38.66 ? 38  ASN A CB  1 
ATOM   284  C CG  . ASN A 1 37  ? 2.592   -26.010 15.429  1.00 42.93 ? 38  ASN A CG  1 
ATOM   285  O OD1 . ASN A 1 37  ? 3.477   -26.653 14.859  1.00 44.91 ? 38  ASN A OD1 1 
ATOM   286  N ND2 . ASN A 1 37  ? 1.812   -26.545 16.363  1.00 50.49 ? 38  ASN A ND2 1 
ATOM   287  N N   . LYS A 1 38  ? 3.820   -21.333 15.925  1.00 35.18 ? 39  LYS A N   1 
ATOM   288  C CA  . LYS A 1 38  ? 3.515   -19.901 15.905  1.00 32.46 ? 39  LYS A CA  1 
ATOM   289  C C   . LYS A 1 38  ? 4.705   -19.113 15.373  1.00 31.97 ? 39  LYS A C   1 
ATOM   290  O O   . LYS A 1 38  ? 5.843   -19.335 15.803  1.00 29.95 ? 39  LYS A O   1 
ATOM   291  C CB  . LYS A 1 38  ? 3.133   -19.381 17.296  1.00 34.48 ? 39  LYS A CB  1 
ATOM   292  C CG  . LYS A 1 38  ? 1.852   -19.972 17.865  1.00 42.12 ? 39  LYS A CG  1 
ATOM   293  C CD  . LYS A 1 38  ? 1.453   -19.253 19.139  1.00 43.76 ? 39  LYS A CD  1 
ATOM   294  C CE  . LYS A 1 38  ? 0.324   -19.970 19.866  1.00 50.84 ? 39  LYS A CE  1 
ATOM   295  N NZ  . LYS A 1 38  ? 0.176   -19.423 21.247  1.00 54.40 ? 39  LYS A NZ  1 
ATOM   296  N N   . LYS A 1 39  ? 4.436   -18.176 14.459  1.00 29.18 ? 40  LYS A N   1 
ATOM   297  C CA  . LYS A 1 39  ? 5.468   -17.365 13.830  1.00 28.43 ? 40  LYS A CA  1 
ATOM   298  C C   . LYS A 1 39  ? 5.563   -16.015 14.534  1.00 28.47 ? 40  LYS A C   1 
ATOM   299  O O   . LYS A 1 39  ? 4.545   -15.444 14.928  1.00 28.69 ? 40  LYS A O   1 
ATOM   300  C CB  . LYS A 1 39  ? 5.169   -17.142 12.342  1.00 26.20 ? 40  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 39  ? 5.140   -18.397 11.461  1.00 29.16 ? 40  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 39  ? 4.979   -17.965 9.999   1.00 31.19 ? 40  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 39  ? 4.860   -19.165 9.053   1.00 32.32 ? 40  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 39  ? 4.831   -18.760 7.599   1.00 29.45 ? 40  LYS A NZ  1 
ATOM   305  N N   . TYR A 1 40  ? 6.788   -15.513 14.689  1.00 24.96 ? 41  TYR A N   1 
ATOM   306  C CA  . TYR A 1 40  ? 7.041   -14.172 15.221  1.00 28.27 ? 41  TYR A CA  1 
ATOM   307  C C   . TYR A 1 40  ? 8.003   -13.469 14.273  1.00 27.66 ? 41  TYR A C   1 
ATOM   308  O O   . TYR A 1 40  ? 9.133   -13.937 14.077  1.00 26.50 ? 41  TYR A O   1 
ATOM   309  C CB  . TYR A 1 40  ? 7.623   -14.235 16.640  1.00 27.25 ? 41  TYR A CB  1 
ATOM   310  C CG  . TYR A 1 40  ? 6.799   -15.062 17.606  1.00 30.01 ? 41  TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 40  ? 6.990   -16.433 17.714  1.00 29.97 ? 41  TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 40  ? 5.817   -14.471 18.399  1.00 31.95 ? 41  TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 40  ? 6.237   -17.199 18.595  1.00 32.95 ? 41  TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 40  ? 5.062   -15.227 19.281  1.00 37.12 ? 41  TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 40  ? 5.276   -16.594 19.371  1.00 36.12 ? 41  TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 40  ? 4.528   -17.349 20.238  1.00 36.43 ? 41  TYR A OH  1 
ATOM   317  N N   . GLU A 1 41  ? 7.562   -12.358 13.683  1.00 25.34 ? 42  GLU A N   1 
ATOM   318  C CA  . GLU A 1 41  ? 8.275   -11.713 12.585  1.00 27.65 ? 42  GLU A CA  1 
ATOM   319  C C   . GLU A 1 41  ? 8.649   -10.279 12.948  1.00 27.12 ? 42  GLU A C   1 
ATOM   320  O O   . GLU A 1 41  ? 7.785   -9.491  13.343  1.00 27.98 ? 42  GLU A O   1 
ATOM   321  C CB  . GLU A 1 41  ? 7.414   -11.735 11.318  1.00 26.09 ? 42  GLU A CB  1 
ATOM   322  C CG  . GLU A 1 41  ? 7.131   -13.156 10.823  1.00 26.69 ? 42  GLU A CG  1 
ATOM   323  C CD  . GLU A 1 41  ? 6.021   -13.219 9.797   1.00 37.03 ? 42  GLU A CD  1 
ATOM   324  O OE1 . GLU A 1 41  ? 5.578   -12.137 9.308   1.00 38.24 ? 42  GLU A OE1 1 
ATOM   325  O OE2 . GLU A 1 41  ? 5.602   -14.360 9.473   1.00 38.15 ? 42  GLU A OE2 1 
ATOM   326  N N   . MET A 1 42  ? 9.932   -9.942  12.798  1.00 24.16 ? 43  MET A N   1 
ATOM   327  C CA  . MET A 1 42  ? 10.445  -8.601  13.069  1.00 27.38 ? 43  MET A CA  1 
ATOM   328  C C   . MET A 1 42  ? 11.107  -8.036  11.818  1.00 25.77 ? 43  MET A C   1 
ATOM   329  O O   . MET A 1 42  ? 11.998  -8.669  11.251  1.00 25.31 ? 43  MET A O   1 
ATOM   330  C CB  . MET A 1 42  ? 11.463  -8.616  14.219  1.00 27.42 ? 43  MET A CB  1 
ATOM   331  C CG  . MET A 1 42  ? 10.857  -8.573  15.610  1.00 32.44 ? 43  MET A CG  1 
ATOM   332  S SD  . MET A 1 42  ? 9.898   -10.020 16.108  1.00 46.76 ? 43  MET A SD  1 
ATOM   333  C CE  . MET A 1 42  ? 10.984  -11.401 15.703  1.00 31.49 ? 43  MET A CE  1 
ATOM   334  N N   . TYR A 1 43  ? 10.698  -6.833  11.408  1.00 24.81 ? 44  TYR A N   1 
ATOM   335  C CA  . TYR A 1 43  ? 11.229  -6.188  10.215  1.00 25.59 ? 44  TYR A CA  1 
ATOM   336  C C   . TYR A 1 43  ? 11.864  -4.855  10.593  1.00 26.23 ? 44  TYR A C   1 
ATOM   337  O O   . TYR A 1 43  ? 11.312  -4.110  11.407  1.00 28.05 ? 44  TYR A O   1 
ATOM   338  C CB  . TYR A 1 43  ? 10.116  -5.980  9.168   1.00 24.38 ? 44  TYR A CB  1 
ATOM   339  C CG  . TYR A 1 43  ? 9.449   -7.289  8.801   1.00 25.11 ? 44  TYR A CG  1 
ATOM   340  C CD1 . TYR A 1 43  ? 10.087  -8.192  7.966   1.00 23.95 ? 44  TYR A CD1 1 
ATOM   341  C CD2 . TYR A 1 43  ? 8.189   -7.630  9.304   1.00 26.79 ? 44  TYR A CD2 1 
ATOM   342  C CE1 . TYR A 1 43  ? 9.502   -9.405  7.632   1.00 23.92 ? 44  TYR A CE1 1 
ATOM   343  C CE2 . TYR A 1 43  ? 7.589   -8.856  8.967   1.00 24.24 ? 44  TYR A CE2 1 
ATOM   344  C CZ  . TYR A 1 43  ? 8.252   -9.725  8.126   1.00 25.69 ? 44  TYR A CZ  1 
ATOM   345  O OH  . TYR A 1 43  ? 7.700   -10.948 7.779   1.00 24.75 ? 44  TYR A OH  1 
ATOM   346  N N   . TYR A 1 44  ? 13.033  -4.566  10.011  1.00 23.33 ? 45  TYR A N   1 
ATOM   347  C CA  . TYR A 1 44  ? 13.773  -3.334  10.274  1.00 24.61 ? 45  TYR A CA  1 
ATOM   348  C C   . TYR A 1 44  ? 14.317  -2.753  8.976   1.00 24.27 ? 45  TYR A C   1 
ATOM   349  O O   . TYR A 1 44  ? 14.784  -3.491  8.107   1.00 24.50 ? 45  TYR A O   1 
ATOM   350  C CB  . TYR A 1 44  ? 14.974  -3.559  11.197  1.00 29.06 ? 45  TYR A CB  1 
ATOM   351  C CG  . TYR A 1 44  ? 14.710  -4.280  12.495  1.00 28.95 ? 45  TYR A CG  1 
ATOM   352  C CD1 . TYR A 1 44  ? 14.231  -3.600  13.608  1.00 33.03 ? 45  TYR A CD1 1 
ATOM   353  C CD2 . TYR A 1 44  ? 14.986  -5.638  12.615  1.00 31.67 ? 45  TYR A CD2 1 
ATOM   354  C CE1 . TYR A 1 44  ? 14.011  -4.262  14.812  1.00 32.29 ? 45  TYR A CE1 1 
ATOM   355  C CE2 . TYR A 1 44  ? 14.777  -6.308  13.809  1.00 33.59 ? 45  TYR A CE2 1 
ATOM   356  C CZ  . TYR A 1 44  ? 14.291  -5.619  14.901  1.00 33.81 ? 45  TYR A CZ  1 
ATOM   357  O OH  . TYR A 1 44  ? 14.077  -6.292  16.084  1.00 31.63 ? 45  TYR A OH  1 
ATOM   358  N N   . GLY A 1 45  ? 14.280  -1.430  8.853   1.00 26.25 ? 46  GLY A N   1 
ATOM   359  C CA  . GLY A 1 45  ? 15.060  -0.785  7.815   1.00 29.83 ? 46  GLY A CA  1 
ATOM   360  C C   . GLY A 1 45  ? 14.473  -0.882  6.414   1.00 28.09 ? 46  GLY A C   1 
ATOM   361  O O   . GLY A 1 45  ? 13.271  -1.096  6.207   1.00 24.53 ? 46  GLY A O   1 
ATOM   362  N N   . LEU A 1 46  ? 15.360  -0.716  5.431   1.00 25.54 ? 47  LEU A N   1 
ATOM   363  C CA  . LEU A 1 46  ? 14.967  -0.486  4.049   1.00 26.95 ? 47  LEU A CA  1 
ATOM   364  C C   . LEU A 1 46  ? 15.255  -1.699  3.170   1.00 29.80 ? 47  LEU A C   1 
ATOM   365  O O   . LEU A 1 46  ? 16.355  -2.272  3.209   1.00 27.45 ? 47  LEU A O   1 
ATOM   366  C CB  . LEU A 1 46  ? 15.670  0.752   3.482   1.00 28.23 ? 47  LEU A CB  1 
ATOM   367  C CG  . LEU A 1 46  ? 15.375  2.057   4.225   1.00 27.60 ? 47  LEU A CG  1 
ATOM   368  C CD1 . LEU A 1 46  ? 16.122  3.249   3.603   1.00 29.85 ? 47  LEU A CD1 1 
ATOM   369  C CD2 . LEU A 1 46  ? 13.858  2.335   4.262   1.00 28.70 ? 47  LEU A CD2 1 
ATOM   370  N N   . GLN A 1 47  ? 14.246  -2.074  2.384   1.00 24.86 ? 48  GLN A N   1 
ATOM   371  C CA  . GLN A 1 47  ? 14.407  -3.024  1.295   1.00 28.34 ? 48  GLN A CA  1 
ATOM   372  C C   . GLN A 1 47  ? 15.277  -2.438  0.193   1.00 34.72 ? 48  GLN A C   1 
ATOM   373  O O   . GLN A 1 47  ? 16.156  -3.120  -0.353  1.00 31.90 ? 48  GLN A O   1 
ATOM   374  C CB  . GLN A 1 47  ? 13.015  -3.379  0.765   1.00 29.14 ? 48  GLN A CB  1 
ATOM   375  C CG  . GLN A 1 47  ? 12.958  -4.229  -0.474  1.00 30.55 ? 48  GLN A CG  1 
ATOM   376  C CD  . GLN A 1 47  ? 11.546  -4.336  -1.004  1.00 29.99 ? 48  GLN A CD  1 
ATOM   377  O OE1 . GLN A 1 47  ? 10.622  -4.735  -0.281  1.00 29.78 ? 48  GLN A OE1 1 
ATOM   378  N NE2 . GLN A 1 47  ? 11.360  -3.970  -2.269  1.00 28.87 ? 48  GLN A NE2 1 
ATOM   379  N N   . SER A 1 48  ? 15.049  -1.166  -0.127  1.00 30.72 ? 49  SER A N   1 
ATOM   380  C CA  . SER A 1 48  ? 15.756  -0.447  -1.178  1.00 35.41 ? 49  SER A CA  1 
ATOM   381  C C   . SER A 1 48  ? 16.032  0.955   -0.659  1.00 36.58 ? 49  SER A C   1 
ATOM   382  O O   . SER A 1 48  ? 15.089  1.683   -0.336  1.00 32.96 ? 49  SER A O   1 
ATOM   383  C CB  . SER A 1 48  ? 14.918  -0.401  -2.460  1.00 34.03 ? 49  SER A CB  1 
ATOM   384  O OG  . SER A 1 48  ? 15.380  0.595   -3.351  1.00 43.08 ? 49  SER A OG  1 
ATOM   385  N N   . VAL A 1 49  ? 17.314  1.318   -0.554  1.00 34.86 ? 50  VAL A N   1 
ATOM   386  C CA  . VAL A 1 49  ? 17.678  2.647   -0.065  1.00 36.93 ? 50  VAL A CA  1 
ATOM   387  C C   . VAL A 1 49  ? 17.226  3.725   -1.044  1.00 39.77 ? 50  VAL A C   1 
ATOM   388  O O   . VAL A 1 49  ? 16.660  4.752   -0.646  1.00 37.61 ? 50  VAL A O   1 
ATOM   389  C CB  . VAL A 1 49  ? 19.194  2.723   0.199   1.00 38.11 ? 50  VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 49  ? 19.589  4.127   0.639   1.00 40.34 ? 50  VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 49  ? 19.599  1.693   1.248   1.00 37.46 ? 50  VAL A CG2 1 
ATOM   392  N N   . GLN A 1 50  ? 17.456  3.504   -2.341  1.00 37.25 ? 51  GLN A N   1 
ATOM   393  C CA  . GLN A 1 50  ? 17.146  4.538   -3.325  1.00 40.73 ? 51  GLN A CA  1 
ATOM   394  C C   . GLN A 1 50  ? 15.642  4.772   -3.448  1.00 38.99 ? 51  GLN A C   1 
ATOM   395  O O   . GLN A 1 50  ? 15.214  5.884   -3.789  1.00 41.77 ? 51  GLN A O   1 
ATOM   396  C CB  . GLN A 1 50  ? 17.745  4.160   -4.682  1.00 44.81 ? 51  GLN A CB  1 
ATOM   397  C CG  . GLN A 1 50  ? 17.040  2.995   -5.368  1.00 50.55 ? 51  GLN A CG  1 
ATOM   398  C CD  . GLN A 1 50  ? 17.879  2.337   -6.451  1.00 54.74 ? 51  GLN A CD  1 
ATOM   399  O OE1 . GLN A 1 50  ? 19.014  1.923   -6.209  1.00 56.23 ? 51  GLN A OE1 1 
ATOM   400  N NE2 . GLN A 1 50  ? 17.314  2.224   -7.650  1.00 54.29 ? 51  GLN A NE2 1 
ATOM   401  N N   . ASP A 1 51  ? 14.834  3.753   -3.169  1.00 38.40 ? 52  ASP A N   1 
ATOM   402  C CA  . ASP A 1 51  ? 13.381  3.843   -3.262  1.00 39.51 ? 52  ASP A CA  1 
ATOM   403  C C   . ASP A 1 51  ? 12.714  4.183   -1.935  1.00 34.71 ? 52  ASP A C   1 
ATOM   404  O O   . ASP A 1 51  ? 11.511  4.451   -1.924  1.00 33.43 ? 52  ASP A O   1 
ATOM   405  C CB  . ASP A 1 51  ? 12.801  2.519   -3.783  1.00 40.24 ? 52  ASP A CB  1 
ATOM   406  C CG  . ASP A 1 51  ? 13.176  2.239   -5.234  1.00 45.78 ? 52  ASP A CG  1 
ATOM   407  O OD1 . ASP A 1 51  ? 12.826  3.051   -6.115  1.00 47.85 ? 52  ASP A OD1 1 
ATOM   408  O OD2 . ASP A 1 51  ? 13.835  1.209   -5.491  1.00 47.65 ? 52  ASP A OD2 1 
ATOM   409  N N   . LYS A 1 52  ? 13.464  4.171   -0.827  1.00 31.33 ? 53  LYS A N   1 
ATOM   410  C CA  . LYS A 1 52  ? 12.913  4.309   0.528   1.00 29.96 ? 53  LYS A CA  1 
ATOM   411  C C   . LYS A 1 52  ? 11.754  3.337   0.777   1.00 30.85 ? 53  LYS A C   1 
ATOM   412  O O   . LYS A 1 52  ? 10.764  3.663   1.436   1.00 29.57 ? 53  LYS A O   1 
ATOM   413  C CB  . LYS A 1 52  ? 12.494  5.755   0.805   1.00 31.75 ? 53  LYS A CB  1 
ATOM   414  C CG  . LYS A 1 52  ? 13.665  6.717   0.924   1.00 33.26 ? 53  LYS A CG  1 
ATOM   415  C CD  . LYS A 1 52  ? 14.393  6.585   2.262   1.00 34.88 ? 53  LYS A CD  1 
ATOM   416  C CE  . LYS A 1 52  ? 15.239  7.834   2.551   1.00 39.34 ? 53  LYS A CE  1 
ATOM   417  N NZ  . LYS A 1 52  ? 15.950  7.762   3.866   1.00 36.65 ? 53  LYS A NZ  1 
ATOM   418  N N   . LYS A 1 53  ? 11.880  2.126   0.252   1.00 31.84 ? 54  LYS A N   1 
ATOM   419  C CA  . LYS A 1 53  ? 10.906  1.071   0.491   1.00 29.81 ? 54  LYS A CA  1 
ATOM   420  C C   . LYS A 1 53  ? 11.342  0.289   1.732   1.00 29.10 ? 54  LYS A C   1 
ATOM   421  O O   . LYS A 1 53  ? 12.464  -0.235  1.785   1.00 29.43 ? 54  LYS A O   1 
ATOM   422  C CB  . LYS A 1 53  ? 10.802  0.156   -0.732  1.00 33.24 ? 54  LYS A CB  1 
ATOM   423  C CG  . LYS A 1 53  ? 9.894   -1.054  -0.569  1.00 29.31 ? 54  LYS A CG  1 
ATOM   424  C CD  . LYS A 1 53  ? 8.433   -0.703  -0.797  1.00 33.91 ? 54  LYS A CD  1 
ATOM   425  C CE  . LYS A 1 53  ? 7.563   -1.948  -0.683  1.00 39.84 ? 54  LYS A CE  1 
ATOM   426  N NZ  . LYS A 1 53  ? 6.169   -1.664  -0.238  1.00 44.29 ? 54  LYS A NZ  1 
ATOM   427  N N   . ALA A 1 54  ? 10.474  0.238   2.737   1.00 26.23 ? 55  ALA A N   1 
ATOM   428  C CA  . ALA A 1 54  ? 10.798  -0.436  3.987   1.00 26.21 ? 55  ALA A CA  1 
ATOM   429  C C   . ALA A 1 54  ? 10.658  -1.957  3.852   1.00 24.69 ? 55  ALA A C   1 
ATOM   430  O O   . ALA A 1 54  ? 9.748   -2.450  3.181   1.00 25.10 ? 55  ALA A O   1 
ATOM   431  C CB  . ALA A 1 54  ? 9.890   0.066   5.103   1.00 25.96 ? 55  ALA A CB  1 
ATOM   432  N N   . VAL A 1 55  ? 11.553  -2.690  4.519   1.00 23.81 ? 56  VAL A N   1 
ATOM   433  C CA  . VAL A 1 55  ? 11.412  -4.150  4.639   1.00 22.96 ? 56  VAL A CA  1 
ATOM   434  C C   . VAL A 1 55  ? 10.041  -4.491  5.218   1.00 23.25 ? 56  VAL A C   1 
ATOM   435  O O   . VAL A 1 55  ? 9.558   -3.833  6.146   1.00 23.60 ? 56  VAL A O   1 
ATOM   436  C CB  . VAL A 1 55  ? 12.529  -4.729  5.524   1.00 22.36 ? 56  VAL A CB  1 
ATOM   437  C CG1 . VAL A 1 55  ? 12.297  -6.235  5.830   1.00 21.61 ? 56  VAL A CG1 1 
ATOM   438  C CG2 . VAL A 1 55  ? 13.894  -4.531  4.887   1.00 22.31 ? 56  VAL A CG2 1 
ATOM   439  N N   . ASN A 1 56  ? 9.399   -5.524  4.670   1.00 25.54 ? 57  ASN A N   1 
ATOM   440  C CA  . ASN A 1 56  ? 8.098   -5.952  5.171   1.00 24.14 ? 57  ASN A CA  1 
ATOM   441  C C   . ASN A 1 56  ? 7.919   -7.453  4.916   1.00 24.25 ? 57  ASN A C   1 
ATOM   442  O O   . ASN A 1 56  ? 8.818   -8.139  4.416   1.00 23.21 ? 57  ASN A O   1 
ATOM   443  C CB  . ASN A 1 56  ? 6.970   -5.131  4.537   1.00 25.33 ? 57  ASN A CB  1 
ATOM   444  C CG  . ASN A 1 56  ? 6.911   -5.303  3.025   1.00 28.32 ? 57  ASN A CG  1 
ATOM   445  O OD1 . ASN A 1 56  ? 6.406   -6.304  2.533   1.00 30.22 ? 57  ASN A OD1 1 
ATOM   446  N ND2 . ASN A 1 56  ? 7.443   -4.330  2.283   1.00 29.36 ? 57  ASN A ND2 1 
ATOM   447  N N   . SER A 1 57  ? 6.731   -7.966  5.250   1.00 23.09 ? 58  SER A N   1 
ATOM   448  C CA  . SER A 1 57  ? 6.487   -9.406  5.111   1.00 22.61 ? 58  SER A CA  1 
ATOM   449  C C   . SER A 1 57  ? 6.520   -9.890  3.660   1.00 23.56 ? 58  SER A C   1 
ATOM   450  O O   . SER A 1 57  ? 6.666   -11.100 3.430   1.00 23.17 ? 58  SER A O   1 
ATOM   451  C CB  . SER A 1 57  ? 5.148   -9.767  5.751   1.00 26.19 ? 58  SER A CB  1 
ATOM   452  O OG  . SER A 1 57  ? 4.100   -8.981  5.215   1.00 29.34 ? 58  SER A OG  1 
ATOM   453  N N   . SER A 1 58  ? 6.400   -8.984  2.679   1.00 25.00 ? 59  SER A N   1 
ATOM   454  C CA  . SER A 1 58  ? 6.512   -9.342  1.268   1.00 24.19 ? 59  SER A CA  1 
ATOM   455  C C   . SER A 1 58  ? 7.921   -9.191  0.708   1.00 22.75 ? 59  SER A C   1 
ATOM   456  O O   . SER A 1 58  ? 8.155   -9.588  -0.440  1.00 25.80 ? 59  SER A O   1 
ATOM   457  C CB  . SER A 1 58  ? 5.566   -8.494  0.411   1.00 28.81 ? 59  SER A CB  1 
ATOM   458  O OG  . SER A 1 58  ? 4.211   -8.768  0.717   1.00 33.80 ? 59  SER A OG  1 
ATOM   459  N N   . THR A 1 59  ? 8.863   -8.649  1.473   1.00 22.77 ? 60  THR A N   1 
ATOM   460  C CA  . THR A 1 59  ? 10.211  -8.448  0.945   1.00 22.76 ? 60  THR A CA  1 
ATOM   461  C C   . THR A 1 59  ? 10.868  -9.778  0.589   1.00 25.06 ? 60  THR A C   1 
ATOM   462  O O   . THR A 1 59  ? 10.911  -10.710 1.404   1.00 21.56 ? 60  THR A O   1 
ATOM   463  C CB  . THR A 1 59  ? 11.081  -7.698  1.947   1.00 21.69 ? 60  THR A CB  1 
ATOM   464  O OG1 . THR A 1 59  ? 10.531  -6.387  2.172   1.00 22.98 ? 60  THR A OG1 1 
ATOM   465  C CG2 . THR A 1 59  ? 12.484  -7.545  1.389   1.00 22.20 ? 60  THR A CG2 1 
ATOM   466  N N   . ILE A 1 60  ? 11.409  -9.846  -0.626  1.00 23.18 ? 61  ILE A N   1 
ATOM   467  C CA  . ILE A 1 60  ? 12.105  -11.021 -1.134  1.00 22.42 ? 61  ILE A CA  1 
ATOM   468  C C   . ILE A 1 60  ? 13.608  -10.760 -1.029  1.00 23.78 ? 61  ILE A C   1 
ATOM   469  O O   . ILE A 1 60  ? 14.109  -9.772  -1.583  1.00 24.27 ? 61  ILE A O   1 
ATOM   470  C CB  . ILE A 1 60  ? 11.687  -11.313 -2.588  1.00 21.70 ? 61  ILE A CB  1 
ATOM   471  C CG1 . ILE A 1 60  ? 10.194  -11.641 -2.666  1.00 22.06 ? 61  ILE A CG1 1 
ATOM   472  C CG2 . ILE A 1 60  ? 12.518  -12.432 -3.185  1.00 21.47 ? 61  ILE A CG2 1 
ATOM   473  C CD1 . ILE A 1 60  ? 9.604   -11.517 -4.078  1.00 23.96 ? 61  ILE A CD1 1 
ATOM   474  N N   . PHE A 1 61  ? 14.322  -11.622 -0.295  1.00 20.27 ? 62  PHE A N   1 
ATOM   475  C CA  . PHE A 1 61  ? 15.765  -11.529 -0.088  1.00 20.93 ? 62  PHE A CA  1 
ATOM   476  C C   . PHE A 1 61  ? 16.500  -12.645 -0.825  1.00 25.80 ? 62  PHE A C   1 
ATOM   477  O O   . PHE A 1 61  ? 16.016  -13.777 -0.908  1.00 23.98 ? 62  PHE A O   1 
ATOM   478  C CB  . PHE A 1 61  ? 16.154  -11.664 1.392   1.00 21.41 ? 62  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 61  ? 15.682  -10.541 2.292   1.00 22.92 ? 62  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 61  ? 14.411  -10.565 2.848   1.00 21.56 ? 62  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 61  ? 16.550  -9.515  2.649   1.00 25.67 ? 62  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 61  ? 13.988  -9.553  3.713   1.00 22.82 ? 62  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 61  ? 16.143  -8.502  3.513   1.00 24.11 ? 62  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 61  ? 14.846  -8.522  4.045   1.00 25.19 ? 62  PHE A CZ  1 
ATOM   485  N N   . GLU A 1 62  ? 17.721  -12.352 -1.273  1.00 26.07 ? 63  GLU A N   1 
ATOM   486  C CA  . GLU A 1 62  ? 18.591  -13.408 -1.779  1.00 27.33 ? 63  GLU A CA  1 
ATOM   487  C C   . GLU A 1 62  ? 19.073  -14.298 -0.634  1.00 23.53 ? 63  GLU A C   1 
ATOM   488  O O   . GLU A 1 62  ? 19.485  -13.812 0.419   1.00 22.30 ? 63  GLU A O   1 
ATOM   489  C CB  . GLU A 1 62  ? 19.765  -12.784 -2.537  1.00 28.02 ? 63  GLU A CB  1 
ATOM   490  C CG  . GLU A 1 62  ? 19.293  -12.123 -3.840  1.00 33.33 ? 63  GLU A CG  1 
ATOM   491  C CD  . GLU A 1 62  ? 20.230  -11.041 -4.366  1.00 48.00 ? 63  GLU A CD  1 
ATOM   492  O OE1 . GLU A 1 62  ? 21.342  -10.881 -3.812  1.00 48.14 ? 63  GLU A OE1 1 
ATOM   493  O OE2 . GLU A 1 62  ? 19.845  -10.343 -5.341  1.00 50.40 ? 63  GLU A OE2 1 
ATOM   494  N N   . LEU A 1 63  ? 18.996  -15.616 -0.819  1.00 21.53 ? 64  LEU A N   1 
ATOM   495  C CA  . LEU A 1 63  ? 19.382  -16.511 0.262   1.00 22.56 ? 64  LEU A CA  1 
ATOM   496  C C   . LEU A 1 63  ? 20.864  -16.848 0.270   1.00 22.85 ? 64  LEU A C   1 
ATOM   497  O O   . LEU A 1 63  ? 21.353  -17.351 1.286   1.00 22.80 ? 64  LEU A O   1 
ATOM   498  C CB  . LEU A 1 63  ? 18.577  -17.812 0.201   1.00 19.48 ? 64  LEU A CB  1 
ATOM   499  C CG  . LEU A 1 63  ? 17.051  -17.699 0.362   1.00 19.31 ? 64  LEU A CG  1 
ATOM   500  C CD1 . LEU A 1 63  ? 16.449  -19.102 0.447   1.00 22.32 ? 64  LEU A CD1 1 
ATOM   501  C CD2 . LEU A 1 63  ? 16.677  -16.874 1.596   1.00 21.06 ? 64  LEU A CD2 1 
ATOM   502  N N   . GLY A 1 64  ? 21.581  -16.589 -0.822  1.00 21.32 ? 65  GLY A N   1 
ATOM   503  C CA  . GLY A 1 64  ? 22.974  -17.010 -0.885  1.00 24.10 ? 65  GLY A CA  1 
ATOM   504  C C   . GLY A 1 64  ? 23.106  -18.514 -0.711  1.00 21.46 ? 65  GLY A C   1 
ATOM   505  O O   . GLY A 1 64  ? 22.284  -19.298 -1.203  1.00 18.16 ? 65  GLY A O   1 
ATOM   506  N N   . SER A 1 65  ? 24.144  -18.920 0.032   1.00 21.00 ? 66  SER A N   1 
ATOM   507  C CA  . SER A 1 65  ? 24.435  -20.335 0.268   1.00 22.94 ? 66  SER A CA  1 
ATOM   508  C C   . SER A 1 65  ? 23.296  -21.111 0.918   1.00 22.77 ? 66  SER A C   1 
ATOM   509  O O   . SER A 1 65  ? 23.281  -22.350 0.830   1.00 20.29 ? 66  SER A O   1 
ATOM   510  C CB  . SER A 1 65  ? 25.671  -20.472 1.155   1.00 30.21 ? 66  SER A CB  1 
ATOM   511  O OG  . SER A 1 65  ? 26.792  -20.710 0.357   1.00 34.11 ? 66  SER A OG  1 
ATOM   512  N N   . VAL A 1 66  ? 22.376  -20.442 1.618   1.00 19.93 ? 67  VAL A N   1 
ATOM   513  C CA  . VAL A 1 66  ? 21.240  -21.160 2.201   1.00 17.55 ? 67  VAL A CA  1 
ATOM   514  C C   . VAL A 1 66  ? 20.377  -21.777 1.099   1.00 18.29 ? 67  VAL A C   1 
ATOM   515  O O   . VAL A 1 66  ? 19.602  -22.710 1.356   1.00 22.50 ? 67  VAL A O   1 
ATOM   516  C CB  . VAL A 1 66  ? 20.471  -20.209 3.156   1.00 19.53 ? 67  VAL A CB  1 
ATOM   517  C CG1 . VAL A 1 66  ? 19.051  -20.726 3.524   1.00 17.55 ? 67  VAL A CG1 1 
ATOM   518  C CG2 . VAL A 1 66  ? 21.272  -20.010 4.429   1.00 22.34 ? 67  VAL A CG2 1 
ATOM   519  N N   . SER A 1 67  ? 20.562  -21.336 -0.152  1.00 17.71 ? 68  SER A N   1 
ATOM   520  C CA  . SER A 1 67  ? 19.912  -21.982 -1.290  1.00 15.03 ? 68  SER A CA  1 
ATOM   521  C C   . SER A 1 67  ? 20.198  -23.480 -1.346  1.00 17.73 ? 68  SER A C   1 
ATOM   522  O O   . SER A 1 67  ? 19.371  -24.252 -1.843  1.00 19.82 ? 68  SER A O   1 
ATOM   523  C CB  . SER A 1 67  ? 20.372  -21.335 -2.599  1.00 17.82 ? 68  SER A CB  1 
ATOM   524  O OG  . SER A 1 67  ? 20.075  -19.946 -2.631  1.00 17.60 ? 68  SER A OG  1 
ATOM   525  N N   . LYS A 1 68  ? 21.377  -23.902 -0.878  1.00 17.30 ? 69  LYS A N   1 
ATOM   526  C CA  . LYS A 1 68  ? 21.750  -25.315 -0.918  1.00 17.44 ? 69  LYS A CA  1 
ATOM   527  C C   . LYS A 1 68  ? 20.788  -26.201 -0.137  1.00 16.70 ? 69  LYS A C   1 
ATOM   528  O O   . LYS A 1 68  ? 20.686  -27.401 -0.428  1.00 16.90 ? 69  LYS A O   1 
ATOM   529  C CB  . LYS A 1 68  ? 23.172  -25.482 -0.381  1.00 17.79 ? 69  LYS A CB  1 
ATOM   530  C CG  . LYS A 1 68  ? 24.209  -24.777 -1.232  1.00 16.56 ? 69  LYS A CG  1 
ATOM   531  C CD  . LYS A 1 68  ? 25.607  -24.883 -0.590  1.00 21.75 ? 69  LYS A CD  1 
ATOM   532  C CE  . LYS A 1 68  ? 26.687  -24.273 -1.493  1.00 21.72 ? 69  LYS A CE  1 
ATOM   533  N NZ  . LYS A 1 68  ? 26.575  -22.791 -1.589  1.00 22.15 ? 69  LYS A NZ  1 
ATOM   534  N N   . LEU A 1 69  ? 20.108  -25.651 0.873   1.00 17.57 ? 70  LEU A N   1 
ATOM   535  C CA  . LEU A 1 69  ? 19.100  -26.424 1.600   1.00 18.79 ? 70  LEU A CA  1 
ATOM   536  C C   . LEU A 1 69  ? 17.948  -26.831 0.695   1.00 20.32 ? 70  LEU A C   1 
ATOM   537  O O   . LEU A 1 69  ? 17.352  -27.894 0.892   1.00 19.21 ? 70  LEU A O   1 
ATOM   538  C CB  . LEU A 1 69  ? 18.559  -25.630 2.787   1.00 18.13 ? 70  LEU A CB  1 
ATOM   539  C CG  . LEU A 1 69  ? 19.583  -25.191 3.841   1.00 19.77 ? 70  LEU A CG  1 
ATOM   540  C CD1 . LEU A 1 69  ? 18.874  -24.433 4.984   1.00 16.51 ? 70  LEU A CD1 1 
ATOM   541  C CD2 . LEU A 1 69  ? 20.383  -26.396 4.349   1.00 18.20 ? 70  LEU A CD2 1 
ATOM   542  N N   . PHE A 1 70  ? 17.628  -26.019 -0.313  1.00 18.27 ? 71  PHE A N   1 
ATOM   543  C CA  . PHE A 1 70  ? 16.567  -26.416 -1.235  1.00 16.39 ? 71  PHE A CA  1 
ATOM   544  C C   . PHE A 1 70  ? 17.064  -27.408 -2.276  1.00 18.69 ? 71  PHE A C   1 
ATOM   545  O O   . PHE A 1 70  ? 16.328  -28.322 -2.658  1.00 18.36 ? 71  PHE A O   1 
ATOM   546  C CB  . PHE A 1 70  ? 15.967  -25.165 -1.887  1.00 19.72 ? 71  PHE A CB  1 
ATOM   547  C CG  . PHE A 1 70  ? 15.182  -24.333 -0.925  1.00 21.05 ? 71  PHE A CG  1 
ATOM   548  C CD1 . PHE A 1 70  ? 13.916  -24.747 -0.522  1.00 21.40 ? 71  PHE A CD1 1 
ATOM   549  C CD2 . PHE A 1 70  ? 15.725  -23.182 -0.367  1.00 21.10 ? 71  PHE A CD2 1 
ATOM   550  C CE1 . PHE A 1 70  ? 13.185  -24.009 0.403   1.00 21.16 ? 71  PHE A CE1 1 
ATOM   551  C CE2 . PHE A 1 70  ? 14.999  -22.425 0.563   1.00 22.96 ? 71  PHE A CE2 1 
ATOM   552  C CZ  . PHE A 1 70  ? 13.715  -22.843 0.942   1.00 20.53 ? 71  PHE A CZ  1 
ATOM   553  N N   . THR A 1 71  ? 18.318  -27.269 -2.712  1.00 16.25 ? 72  THR A N   1 
ATOM   554  C CA  . THR A 1 71  ? 18.949  -28.294 -3.532  1.00 14.47 ? 72  THR A CA  1 
ATOM   555  C C   . THR A 1 71  ? 18.962  -29.632 -2.806  1.00 14.44 ? 72  THR A C   1 
ATOM   556  O O   . THR A 1 71  ? 18.694  -30.680 -3.408  1.00 15.74 ? 72  THR A O   1 
ATOM   557  C CB  . THR A 1 71  ? 20.379  -27.849 -3.872  1.00 16.37 ? 72  THR A CB  1 
ATOM   558  O OG1 . THR A 1 71  ? 20.336  -26.543 -4.458  1.00 17.08 ? 72  THR A OG1 1 
ATOM   559  C CG2 . THR A 1 71  ? 21.058  -28.823 -4.838  1.00 18.05 ? 72  THR A CG2 1 
ATOM   560  N N   . ALA A 1 72  ? 19.274  -29.613 -1.504  1.00 15.29 ? 73  ALA A N   1 
ATOM   561  C CA  . ALA A 1 72  ? 19.295  -30.837 -0.712  1.00 16.63 ? 73  ALA A CA  1 
ATOM   562  C C   . ALA A 1 72  ? 17.921  -31.462 -0.633  1.00 17.40 ? 73  ALA A C   1 
ATOM   563  O O   . ALA A 1 72  ? 17.777  -32.688 -0.772  1.00 16.16 ? 73  ALA A O   1 
ATOM   564  C CB  . ALA A 1 72  ? 19.808  -30.553 0.698   1.00 17.75 ? 73  ALA A CB  1 
ATOM   565  N N   . THR A 1 73  ? 16.905  -30.639 -0.398  1.00 15.91 ? 74  THR A N   1 
ATOM   566  C CA  . THR A 1 73  ? 15.542  -31.151 -0.324  1.00 16.17 ? 74  THR A CA  1 
ATOM   567  C C   . THR A 1 73  ? 15.113  -31.740 -1.664  1.00 17.04 ? 74  THR A C   1 
ATOM   568  O O   . THR A 1 73  ? 14.495  -32.811 -1.704  1.00 17.01 ? 74  THR A O   1 
ATOM   569  C CB  . THR A 1 73  ? 14.604  -30.033 0.128   1.00 17.49 ? 74  THR A CB  1 
ATOM   570  O OG1 . THR A 1 73  ? 15.041  -29.537 1.413   1.00 17.08 ? 74  THR A OG1 1 
ATOM   571  C CG2 . THR A 1 73  ? 13.172  -30.556 0.253   1.00 16.65 ? 74  THR A CG2 1 
ATOM   572  N N   . ALA A 1 74  ? 15.443  -31.061 -2.776  1.00 16.62 ? 75  ALA A N   1 
ATOM   573  C CA  . ALA A 1 74  ? 15.129  -31.623 -4.091  1.00 16.90 ? 75  ALA A CA  1 
ATOM   574  C C   . ALA A 1 74  ? 15.813  -32.971 -4.298  1.00 17.69 ? 75  ALA A C   1 
ATOM   575  O O   . ALA A 1 74  ? 15.226  -33.890 -4.882  1.00 18.57 ? 75  ALA A O   1 
ATOM   576  C CB  . ALA A 1 74  ? 15.519  -30.645 -5.206  1.00 18.12 ? 75  ALA A CB  1 
ATOM   577  N N   . GLY A 1 75  ? 17.061  -33.109 -3.843  1.00 16.82 ? 76  GLY A N   1 
ATOM   578  C CA  . GLY A 1 75  ? 17.739  -34.389 -3.975  1.00 17.20 ? 76  GLY A CA  1 
ATOM   579  C C   . GLY A 1 75  ? 17.121  -35.468 -3.105  1.00 19.10 ? 76  GLY A C   1 
ATOM   580  O O   . GLY A 1 75  ? 17.008  -36.623 -3.529  1.00 15.23 ? 76  GLY A O   1 
ATOM   581  N N   . GLY A 1 76  ? 16.721  -35.109 -1.876  1.00 15.64 ? 77  GLY A N   1 
ATOM   582  C CA  . GLY A 1 76  ? 16.032  -36.070 -1.027  1.00 18.85 ? 77  GLY A CA  1 
ATOM   583  C C   . GLY A 1 76  ? 14.714  -36.496 -1.639  1.00 18.82 ? 77  GLY A C   1 
ATOM   584  O O   . GLY A 1 76  ? 14.310  -37.661 -1.515  1.00 19.20 ? 77  GLY A O   1 
ATOM   585  N N   . TYR A 1 77  ? 14.068  -35.575 -2.357  1.00 17.01 ? 78  TYR A N   1 
ATOM   586  C CA  . TYR A 1 77  ? 12.803  -35.859 -3.030  1.00 16.39 ? 78  TYR A CA  1 
ATOM   587  C C   . TYR A 1 77  ? 13.004  -36.822 -4.190  1.00 19.37 ? 78  TYR A C   1 
ATOM   588  O O   . TYR A 1 77  ? 12.265  -37.801 -4.331  1.00 20.34 ? 78  TYR A O   1 
ATOM   589  C CB  . TYR A 1 77  ? 12.186  -34.555 -3.536  1.00 17.09 ? 78  TYR A CB  1 
ATOM   590  C CG  . TYR A 1 77  ? 10.815  -34.700 -4.186  1.00 18.09 ? 78  TYR A CG  1 
ATOM   591  C CD1 . TYR A 1 77  ? 10.690  -34.965 -5.552  1.00 20.56 ? 78  TYR A CD1 1 
ATOM   592  C CD2 . TYR A 1 77  ? 9.655   -34.533 -3.441  1.00 21.00 ? 78  TYR A CD2 1 
ATOM   593  C CE1 . TYR A 1 77  ? 9.447   -35.091 -6.146  1.00 23.38 ? 78  TYR A CE1 1 
ATOM   594  C CE2 . TYR A 1 77  ? 8.408   -34.632 -4.031  1.00 21.90 ? 78  TYR A CE2 1 
ATOM   595  C CZ  . TYR A 1 77  ? 8.309   -34.914 -5.377  1.00 25.43 ? 78  TYR A CZ  1 
ATOM   596  O OH  . TYR A 1 77  ? 7.065   -35.012 -5.956  1.00 28.68 ? 78  TYR A OH  1 
ATOM   597  N N   . ALA A 1 78  ? 13.978  -36.527 -5.054  1.00 18.22 ? 79  ALA A N   1 
ATOM   598  C CA  . ALA A 1 78  ? 14.280  -37.403 -6.182  1.00 18.25 ? 79  ALA A CA  1 
ATOM   599  C C   . ALA A 1 78  ? 14.659  -38.802 -5.712  1.00 19.17 ? 79  ALA A C   1 
ATOM   600  O O   . ALA A 1 78  ? 14.221  -39.802 -6.291  1.00 20.23 ? 79  ALA A O   1 
ATOM   601  C CB  . ALA A 1 78  ? 15.418  -36.802 -7.013  1.00 20.14 ? 79  ALA A CB  1 
ATOM   602  N N   . LYS A 1 79  ? 15.494  -38.890 -4.674  1.00 18.73 ? 80  LYS A N   1 
ATOM   603  C CA  . LYS A 1 79  ? 15.928  -40.198 -4.194  1.00 20.07 ? 80  LYS A CA  1 
ATOM   604  C C   . LYS A 1 79  ? 14.754  -41.001 -3.636  1.00 23.36 ? 80  LYS A C   1 
ATOM   605  O O   . LYS A 1 79  ? 14.636  -42.206 -3.902  1.00 20.58 ? 80  LYS A O   1 
ATOM   606  C CB  . LYS A 1 79  ? 17.045  -40.022 -3.153  1.00 19.64 ? 80  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 79  ? 17.573  -41.313 -2.536  1.00 20.34 ? 80  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 79  ? 16.898  -41.593 -1.196  1.00 23.03 ? 80  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 79  ? 17.407  -42.876 -0.508  1.00 24.79 ? 80  LYS A CE  1 
ATOM   610  N NZ  . LYS A 1 79  ? 16.574  -43.138 0.715   1.00 25.41 ? 80  LYS A NZ  1 
ATOM   611  N N   . ASN A 1 80  ? 13.861  -40.357 -2.877  1.00 18.38 ? 81  ASN A N   1 
ATOM   612  C CA  . ASN A 1 80  ? 12.777  -41.106 -2.259  1.00 21.73 ? 81  ASN A CA  1 
ATOM   613  C C   . ASN A 1 80  ? 11.651  -41.431 -3.234  1.00 22.81 ? 81  ASN A C   1 
ATOM   614  O O   . ASN A 1 80  ? 10.777  -42.250 -2.908  1.00 22.90 ? 81  ASN A O   1 
ATOM   615  C CB  . ASN A 1 80  ? 12.267  -40.350 -1.029  1.00 20.87 ? 81  ASN A CB  1 
ATOM   616  C CG  . ASN A 1 80  ? 13.176  -40.564 0.179   1.00 26.57 ? 81  ASN A CG  1 
ATOM   617  O OD1 . ASN A 1 80  ? 13.926  -39.661 0.588   1.00 26.21 ? 81  ASN A OD1 1 
ATOM   618  N ND2 . ASN A 1 80  ? 13.142  -41.777 0.735   1.00 21.42 ? 81  ASN A ND2 1 
ATOM   619  N N   . LYS A 1 81  ? 11.675  -40.843 -4.424  1.00 21.89 ? 82  LYS A N   1 
ATOM   620  C CA  . LYS A 1 81  ? 10.796  -41.235 -5.517  1.00 22.21 ? 82  LYS A CA  1 
ATOM   621  C C   . LYS A 1 81  ? 11.439  -42.246 -6.459  1.00 23.55 ? 82  LYS A C   1 
ATOM   622  O O   . LYS A 1 81  ? 10.816  -42.625 -7.456  1.00 26.73 ? 82  LYS A O   1 
ATOM   623  C CB  . LYS A 1 81  ? 10.365  -39.999 -6.308  1.00 24.67 ? 82  LYS A CB  1 
ATOM   624  C CG  . LYS A 1 81  ? 9.043   -39.425 -5.836  1.00 30.55 ? 82  LYS A CG  1 
ATOM   625  C CD  . LYS A 1 81  ? 8.385   -38.687 -6.971  1.00 38.00 ? 82  LYS A CD  1 
ATOM   626  C CE  . LYS A 1 81  ? 6.883   -38.637 -6.798  1.00 39.41 ? 82  LYS A CE  1 
ATOM   627  N NZ  . LYS A 1 81  ? 6.316   -37.746 -7.846  1.00 42.38 ? 82  LYS A NZ  1 
ATOM   628  N N   . GLY A 1 82  ? 12.669  -42.673 -6.182  1.00 25.59 ? 83  GLY A N   1 
ATOM   629  C CA  . GLY A 1 82  ? 13.347  -43.631 -7.029  1.00 24.29 ? 83  GLY A CA  1 
ATOM   630  C C   . GLY A 1 82  ? 13.923  -43.074 -8.314  1.00 24.73 ? 83  GLY A C   1 
ATOM   631  O O   . GLY A 1 82  ? 14.344  -43.862 -9.169  1.00 22.83 ? 83  GLY A O   1 
ATOM   632  N N   . LYS A 1 83  ? 13.959  -41.743 -8.476  1.00 18.69 ? 84  LYS A N   1 
ATOM   633  C CA  . LYS A 1 83  ? 14.520  -41.123 -9.676  1.00 21.77 ? 84  LYS A CA  1 
ATOM   634  C C   . LYS A 1 83  ? 16.047  -41.154 -9.689  1.00 21.01 ? 84  LYS A C   1 
ATOM   635  O O   . LYS A 1 83  ? 16.649  -41.116 -10.769 1.00 20.07 ? 84  LYS A O   1 
ATOM   636  C CB  . LYS A 1 83  ? 14.041  -39.672 -9.800  1.00 20.65 ? 84  LYS A CB  1 
ATOM   637  C CG  . LYS A 1 83  ? 12.520  -39.516 -9.878  1.00 22.85 ? 84  LYS A CG  1 
ATOM   638  C CD  . LYS A 1 83  ? 11.970  -40.089 -11.157 1.00 25.90 ? 84  LYS A CD  1 
ATOM   639  C CE  . LYS A 1 83  ? 10.440  -39.999 -11.174 1.00 33.13 ? 84  LYS A CE  1 
ATOM   640  N NZ  . LYS A 1 83  ? 9.886   -40.349 -12.497 1.00 37.72 ? 84  LYS A NZ  1 
ATOM   641  N N   . ILE A 1 84  ? 16.678  -41.174 -8.513  1.00 19.39 ? 85  ILE A N   1 
ATOM   642  C CA  . ILE A 1 84  ? 18.117  -41.367 -8.368  1.00 20.64 ? 85  ILE A CA  1 
ATOM   643  C C   . ILE A 1 84  ? 18.357  -42.315 -7.203  1.00 23.45 ? 85  ILE A C   1 
ATOM   644  O O   . ILE A 1 84  ? 17.493  -42.525 -6.347  1.00 19.52 ? 85  ILE A O   1 
ATOM   645  C CB  . ILE A 1 84  ? 18.905  -40.064 -8.096  1.00 18.97 ? 85  ILE A CB  1 
ATOM   646  C CG1 . ILE A 1 84  ? 18.410  -39.403 -6.808  1.00 19.44 ? 85  ILE A CG1 1 
ATOM   647  C CG2 . ILE A 1 84  ? 18.782  -39.077 -9.218  1.00 17.95 ? 85  ILE A CG2 1 
ATOM   648  C CD1 . ILE A 1 84  ? 19.138  -38.129 -6.464  1.00 20.27 ? 85  ILE A CD1 1 
ATOM   649  N N   . SER A 1 85  ? 19.570  -42.852 -7.160  1.00 20.89 ? 86  SER A N   1 
ATOM   650  C CA  . SER A 1 85  ? 20.134  -43.461 -5.969  1.00 19.69 ? 86  SER A CA  1 
ATOM   651  C C   . SER A 1 85  ? 21.402  -42.695 -5.631  1.00 21.84 ? 86  SER A C   1 
ATOM   652  O O   . SER A 1 85  ? 22.125  -42.267 -6.534  1.00 19.44 ? 86  SER A O   1 
ATOM   653  C CB  . SER A 1 85  ? 20.445  -44.949 -6.196  1.00 22.49 ? 86  SER A CB  1 
ATOM   654  O OG  . SER A 1 85  ? 21.340  -45.442 -5.222  1.00 28.82 ? 86  SER A OG  1 
ATOM   655  N N   . PHE A 1 86  ? 21.660  -42.494 -4.336  1.00 20.97 ? 87  PHE A N   1 
ATOM   656  C CA  . PHE A 1 86  ? 22.856  -41.746 -3.961  1.00 20.61 ? 87  PHE A CA  1 
ATOM   657  C C   . PHE A 1 86  ? 24.129  -42.489 -4.340  1.00 21.55 ? 87  PHE A C   1 
ATOM   658  O O   . PHE A 1 86  ? 25.193  -41.867 -4.384  1.00 21.98 ? 87  PHE A O   1 
ATOM   659  C CB  . PHE A 1 86  ? 22.861  -41.430 -2.456  1.00 22.49 ? 87  PHE A CB  1 
ATOM   660  C CG  . PHE A 1 86  ? 21.816  -40.409 -2.027  1.00 20.62 ? 87  PHE A CG  1 
ATOM   661  C CD1 . PHE A 1 86  ? 21.427  -39.377 -2.875  1.00 24.58 ? 87  PHE A CD1 1 
ATOM   662  C CD2 . PHE A 1 86  ? 21.221  -40.502 -0.779  1.00 22.96 ? 87  PHE A CD2 1 
ATOM   663  C CE1 . PHE A 1 86  ? 20.458  -38.456 -2.487  1.00 25.26 ? 87  PHE A CE1 1 
ATOM   664  C CE2 . PHE A 1 86  ? 20.266  -39.590 -0.374  1.00 22.10 ? 87  PHE A CE2 1 
ATOM   665  C CZ  . PHE A 1 86  ? 19.876  -38.558 -1.230  1.00 24.90 ? 87  PHE A CZ  1 
ATOM   666  N N   . ASP A 1 87  ? 24.054  -43.805 -4.595  1.00 18.17 ? 88  ASP A N   1 
ATOM   667  C CA  . ASP A 1 87  ? 25.192  -44.564 -5.106  1.00 20.78 ? 88  ASP A CA  1 
ATOM   668  C C   . ASP A 1 87  ? 25.412  -44.411 -6.609  1.00 20.82 ? 88  ASP A C   1 
ATOM   669  O O   . ASP A 1 87  ? 26.430  -44.898 -7.113  1.00 22.60 ? 88  ASP A O   1 
ATOM   670  C CB  . ASP A 1 87  ? 25.027  -46.053 -4.784  1.00 22.66 ? 88  ASP A CB  1 
ATOM   671  C CG  . ASP A 1 87  ? 25.306  -46.369 -3.334  1.00 33.75 ? 88  ASP A CG  1 
ATOM   672  O OD1 . ASP A 1 87  ? 25.806  -45.475 -2.609  1.00 30.61 ? 88  ASP A OD1 1 
ATOM   673  O OD2 . ASP A 1 87  ? 25.027  -47.519 -2.916  1.00 40.94 ? 88  ASP A OD2 1 
ATOM   674  N N   . ASP A 1 88  ? 24.511  -43.750 -7.335  1.00 21.23 ? 89  ASP A N   1 
ATOM   675  C CA  . ASP A 1 88  ? 24.710  -43.525 -8.762  1.00 23.58 ? 89  ASP A CA  1 
ATOM   676  C C   . ASP A 1 88  ? 25.862  -42.546 -9.010  1.00 21.01 ? 89  ASP A C   1 
ATOM   677  O O   . ASP A 1 88  ? 26.274  -41.782 -8.130  1.00 20.40 ? 89  ASP A O   1 
ATOM   678  C CB  . ASP A 1 88  ? 23.442  -42.962 -9.414  1.00 20.51 ? 89  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 88  ? 22.280  -43.958 -9.448  1.00 24.92 ? 89  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 88  ? 22.484  -45.201 -9.358  1.00 24.78 ? 89  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 88  ? 21.133  -43.482 -9.607  1.00 27.69 ? 89  ASP A OD2 1 
ATOM   682  N N   . THR A 1 89  ? 26.365  -42.542 -10.240 1.00 23.23 ? 90  THR A N   1 
ATOM   683  C CA  . THR A 1 89  ? 27.378  -41.565 -10.628 1.00 18.38 ? 90  THR A CA  1 
ATOM   684  C C   . THR A 1 89  ? 26.802  -40.585 -11.660 1.00 20.83 ? 90  THR A C   1 
ATOM   685  O O   . THR A 1 89  ? 25.757  -40.863 -12.263 1.00 22.09 ? 90  THR A O   1 
ATOM   686  C CB  . THR A 1 89  ? 28.632  -42.291 -11.153 1.00 24.20 ? 90  THR A CB  1 
ATOM   687  O OG1 . THR A 1 89  ? 28.319  -43.093 -12.301 1.00 23.81 ? 90  THR A OG1 1 
ATOM   688  C CG2 . THR A 1 89  ? 29.208  -43.211 -10.063 1.00 25.01 ? 90  THR A CG2 1 
ATOM   689  N N   . PRO A 1 90  ? 27.406  -39.398 -11.845 1.00 20.97 ? 91  PRO A N   1 
ATOM   690  C CA  . PRO A 1 90  ? 26.712  -38.362 -12.644 1.00 22.89 ? 91  PRO A CA  1 
ATOM   691  C C   . PRO A 1 90  ? 26.533  -38.708 -14.124 1.00 22.73 ? 91  PRO A C   1 
ATOM   692  O O   . PRO A 1 90  ? 25.589  -38.202 -14.748 1.00 25.75 ? 91  PRO A O   1 
ATOM   693  C CB  . PRO A 1 90  ? 27.585  -37.109 -12.455 1.00 22.09 ? 91  PRO A CB  1 
ATOM   694  C CG  . PRO A 1 90  ? 28.952  -37.623 -12.113 1.00 20.48 ? 91  PRO A CG  1 
ATOM   695  C CD  . PRO A 1 90  ? 28.682  -38.893 -11.290 1.00 20.71 ? 91  PRO A CD  1 
ATOM   696  N N   . GLY A 1 91  ? 27.391  -39.550 -14.705 1.00 23.75 ? 92  GLY A N   1 
ATOM   697  C CA  . GLY A 1 91  ? 27.258  -39.933 -16.111 1.00 24.09 ? 92  GLY A CA  1 
ATOM   698  C C   . GLY A 1 91  ? 26.060  -40.813 -16.425 1.00 26.27 ? 92  GLY A C   1 
ATOM   699  O O   . GLY A 1 91  ? 25.743  -41.012 -17.606 1.00 24.64 ? 92  GLY A O   1 
ATOM   700  N N   . LYS A 1 92  ? 25.407  -41.360 -15.402 1.00 22.46 ? 93  LYS A N   1 
ATOM   701  C CA  . LYS A 1 92  ? 24.156  -42.074 -15.616 1.00 25.97 ? 93  LYS A CA  1 
ATOM   702  C C   . LYS A 1 92  ? 23.070  -41.143 -16.136 1.00 26.02 ? 93  LYS A C   1 
ATOM   703  O O   . LYS A 1 92  ? 22.165  -41.583 -16.859 1.00 25.37 ? 93  LYS A O   1 
ATOM   704  C CB  . LYS A 1 92  ? 23.720  -42.727 -14.305 1.00 25.16 ? 93  LYS A CB  1 
ATOM   705  C CG  . LYS A 1 92  ? 22.399  -43.477 -14.361 1.00 23.57 ? 93  LYS A CG  1 
ATOM   706  C CD  . LYS A 1 92  ? 22.177  -44.207 -13.032 1.00 28.60 ? 93  LYS A CD  1 
ATOM   707  C CE  . LYS A 1 92  ? 20.875  -44.998 -13.025 1.00 30.90 ? 93  LYS A CE  1 
ATOM   708  N NZ  . LYS A 1 92  ? 21.016  -46.233 -13.823 1.00 43.38 ? 93  LYS A NZ  1 
ATOM   709  N N   . TYR A 1 93  ? 23.155  -39.858 -15.800 1.00 23.28 ? 94  TYR A N   1 
ATOM   710  C CA  . TYR A 1 93  ? 22.135  -38.864 -16.111 1.00 27.16 ? 94  TYR A CA  1 
ATOM   711  C C   . TYR A 1 93  ? 22.609  -37.790 -17.072 1.00 27.46 ? 94  TYR A C   1 
ATOM   712  O O   . TYR A 1 93  ? 21.843  -37.388 -17.955 1.00 24.04 ? 94  TYR A O   1 
ATOM   713  C CB  . TYR A 1 93  ? 21.645  -38.201 -14.822 1.00 23.06 ? 94  TYR A CB  1 
ATOM   714  C CG  . TYR A 1 93  ? 21.136  -39.234 -13.855 1.00 21.79 ? 94  TYR A CG  1 
ATOM   715  C CD1 . TYR A 1 93  ? 19.830  -39.685 -13.925 1.00 23.03 ? 94  TYR A CD1 1 
ATOM   716  C CD2 . TYR A 1 93  ? 21.976  -39.796 -12.907 1.00 20.58 ? 94  TYR A CD2 1 
ATOM   717  C CE1 . TYR A 1 93  ? 19.365  -40.654 -13.070 1.00 22.08 ? 94  TYR A CE1 1 
ATOM   718  C CE2 . TYR A 1 93  ? 21.509  -40.774 -12.027 1.00 21.90 ? 94  TYR A CE2 1 
ATOM   719  C CZ  . TYR A 1 93  ? 20.201  -41.185 -12.117 1.00 21.88 ? 94  TYR A CZ  1 
ATOM   720  O OH  . TYR A 1 93  ? 19.707  -42.161 -11.273 1.00 28.40 ? 94  TYR A OH  1 
ATOM   721  N N   . TRP A 1 94  ? 23.844  -37.314 -16.913 1.00 23.24 ? 95  TRP A N   1 
ATOM   722  C CA  . TRP A 1 94  ? 24.469  -36.369 -17.847 1.00 24.32 ? 95  TRP A CA  1 
ATOM   723  C C   . TRP A 1 94  ? 25.398  -37.201 -18.729 1.00 25.12 ? 95  TRP A C   1 
ATOM   724  O O   . TRP A 1 94  ? 26.559  -37.445 -18.395 1.00 23.37 ? 95  TRP A O   1 
ATOM   725  C CB  . TRP A 1 94  ? 25.203  -35.255 -17.096 1.00 24.26 ? 95  TRP A CB  1 
ATOM   726  C CG  . TRP A 1 94  ? 25.450  -34.004 -17.915 1.00 23.67 ? 95  TRP A CG  1 
ATOM   727  C CD1 . TRP A 1 94  ? 25.184  -33.827 -19.249 1.00 28.34 ? 95  TRP A CD1 1 
ATOM   728  C CD2 . TRP A 1 94  ? 25.997  -32.760 -17.450 1.00 21.33 ? 95  TRP A CD2 1 
ATOM   729  N NE1 . TRP A 1 94  ? 25.532  -32.548 -19.637 1.00 25.71 ? 95  TRP A NE1 1 
ATOM   730  C CE2 . TRP A 1 94  ? 26.030  -31.874 -18.555 1.00 24.46 ? 95  TRP A CE2 1 
ATOM   731  C CE3 . TRP A 1 94  ? 26.448  -32.306 -16.209 1.00 23.11 ? 95  TRP A CE3 1 
ATOM   732  C CZ2 . TRP A 1 94  ? 26.510  -30.556 -18.455 1.00 23.35 ? 95  TRP A CZ2 1 
ATOM   733  C CZ3 . TRP A 1 94  ? 26.930  -31.002 -16.104 1.00 24.41 ? 95  TRP A CZ3 1 
ATOM   734  C CH2 . TRP A 1 94  ? 26.954  -30.137 -17.226 1.00 25.67 ? 95  TRP A CH2 1 
ATOM   735  N N   . LYS A 1 95  ? 24.868  -37.650 -19.871 1.00 23.93 ? 96  LYS A N   1 
ATOM   736  C CA  . LYS A 1 95  ? 25.501  -38.732 -20.620 1.00 25.47 ? 96  LYS A CA  1 
ATOM   737  C C   . LYS A 1 95  ? 26.884  -38.360 -21.131 1.00 26.35 ? 96  LYS A C   1 
ATOM   738  O O   . LYS A 1 95  ? 27.723  -39.247 -21.332 1.00 22.65 ? 96  LYS A O   1 
ATOM   739  C CB  . LYS A 1 95  ? 24.607  -39.150 -21.790 1.00 30.21 ? 96  LYS A CB  1 
ATOM   740  C CG  . LYS A 1 95  ? 23.179  -39.466 -21.380 1.00 36.52 ? 96  LYS A CG  1 
ATOM   741  C CD  . LYS A 1 95  ? 23.088  -40.701 -20.498 1.00 34.46 ? 96  LYS A CD  1 
ATOM   742  C CE  . LYS A 1 95  ? 21.622  -41.124 -20.285 1.00 36.36 ? 96  LYS A CE  1 
ATOM   743  N NZ  . LYS A 1 95  ? 20.920  -41.448 -21.565 1.00 42.95 ? 96  LYS A NZ  1 
ATOM   744  N N   . GLU A 1 96  ? 27.152  -37.062 -21.344 1.00 23.47 ? 97  GLU A N   1 
ATOM   745  C CA  . GLU A 1 96  ? 28.476  -36.663 -21.810 1.00 22.93 ? 97  GLU A CA  1 
ATOM   746  C C   . GLU A 1 96  ? 29.564  -36.858 -20.760 1.00 22.30 ? 97  GLU A C   1 
ATOM   747  O O   . GLU A 1 96  ? 30.745  -36.785 -21.106 1.00 24.86 ? 97  GLU A O   1 
ATOM   748  C CB  . GLU A 1 96  ? 28.466  -35.198 -22.282 1.00 26.64 ? 97  GLU A CB  1 
ATOM   749  C CG  . GLU A 1 96  ? 27.663  -34.969 -23.550 1.00 29.23 ? 97  GLU A CG  1 
ATOM   750  C CD  . GLU A 1 96  ? 26.270  -34.401 -23.288 1.00 40.01 ? 97  GLU A CD  1 
ATOM   751  O OE1 . GLU A 1 96  ? 25.879  -33.447 -24.008 1.00 45.89 ? 97  GLU A OE1 1 
ATOM   752  O OE2 . GLU A 1 96  ? 25.575  -34.887 -22.360 1.00 34.36 ? 97  GLU A OE2 1 
ATOM   753  N N   . LEU A 1 97  ? 29.209  -37.123 -19.504 1.00 20.38 ? 98  LEU A N   1 
ATOM   754  C CA  . LEU A 1 97  ? 30.205  -37.440 -18.487 1.00 21.02 ? 98  LEU A CA  1 
ATOM   755  C C   . LEU A 1 97  ? 30.494  -38.936 -18.380 1.00 22.16 ? 98  LEU A C   1 
ATOM   756  O O   . LEU A 1 97  ? 31.289  -39.338 -17.525 1.00 24.08 ? 98  LEU A O   1 
ATOM   757  C CB  . LEU A 1 97  ? 29.755  -36.913 -17.121 1.00 18.54 ? 98  LEU A CB  1 
ATOM   758  C CG  . LEU A 1 97  ? 29.612  -35.382 -17.045 1.00 19.53 ? 98  LEU A CG  1 
ATOM   759  C CD1 . LEU A 1 97  ? 29.157  -34.941 -15.645 1.00 18.78 ? 98  LEU A CD1 1 
ATOM   760  C CD2 . LEU A 1 97  ? 30.925  -34.709 -17.431 1.00 23.41 ? 98  LEU A CD2 1 
ATOM   761  N N   . LYS A 1 98  ? 29.876  -39.771 -19.200 1.00 24.11 ? 99  LYS A N   1 
ATOM   762  C CA  . LYS A 1 98  ? 30.168  -41.201 -19.122 1.00 25.03 ? 99  LYS A CA  1 
ATOM   763  C C   . LYS A 1 98  ? 31.619  -41.462 -19.493 1.00 26.49 ? 99  LYS A C   1 
ATOM   764  O O   . LYS A 1 98  ? 32.166  -40.819 -20.388 1.00 24.31 ? 99  LYS A O   1 
ATOM   765  C CB  . LYS A 1 98  ? 29.260  -41.988 -20.060 1.00 29.20 ? 99  LYS A CB  1 
ATOM   766  C CG  . LYS A 1 98  ? 27.967  -42.448 -19.435 1.00 35.77 ? 99  LYS A CG  1 
ATOM   767  C CD  . LYS A 1 98  ? 27.415  -43.669 -20.170 1.00 38.64 ? 99  LYS A CD  1 
ATOM   768  C CE  . LYS A 1 98  ? 26.169  -44.206 -19.473 1.00 40.84 ? 99  LYS A CE  1 
ATOM   769  N NZ  . LYS A 1 98  ? 25.093  -43.184 -19.414 1.00 38.27 ? 99  LYS A NZ  1 
ATOM   770  N N   . ASN A 1 99  ? 32.244  -42.431 -18.820 1.00 29.43 ? 100 ASN A N   1 
ATOM   771  C CA  . ASN A 1 99  ? 33.614  -42.840 -19.155 1.00 30.76 ? 100 ASN A CA  1 
ATOM   772  C C   . ASN A 1 99  ? 34.617  -41.705 -18.962 1.00 27.43 ? 100 ASN A C   1 
ATOM   773  O O   . ASN A 1 99  ? 35.641  -41.645 -19.649 1.00 28.18 ? 100 ASN A O   1 
ATOM   774  C CB  . ASN A 1 99  ? 33.718  -43.365 -20.595 1.00 35.40 ? 100 ASN A CB  1 
ATOM   775  C CG  . ASN A 1 99  ? 32.905  -44.605 -20.822 1.00 40.39 ? 100 ASN A CG  1 
ATOM   776  O OD1 . ASN A 1 99  ? 32.657  -45.372 -19.891 1.00 40.70 ? 100 ASN A OD1 1 
ATOM   777  N ND2 . ASN A 1 99  ? 32.471  -44.813 -22.072 1.00 41.37 ? 100 ASN A ND2 1 
ATOM   778  N N   . THR A 1 100 ? 34.325  -40.773 -18.063 1.00 28.17 ? 101 THR A N   1 
ATOM   779  C CA  . THR A 1 100 ? 35.285  -39.768 -17.642 1.00 25.68 ? 101 THR A CA  1 
ATOM   780  C C   . THR A 1 100 ? 35.553  -39.939 -16.150 1.00 22.18 ? 101 THR A C   1 
ATOM   781  O O   . THR A 1 100 ? 34.746  -40.543 -15.434 1.00 21.77 ? 101 THR A O   1 
ATOM   782  C CB  . THR A 1 100 ? 34.782  -38.343 -17.930 1.00 24.52 ? 101 THR A CB  1 
ATOM   783  O OG1 . THR A 1 100 ? 33.691  -38.027 -17.052 1.00 22.87 ? 101 THR A OG1 1 
ATOM   784  C CG2 . THR A 1 100 ? 34.330  -38.233 -19.368 1.00 23.04 ? 101 THR A CG2 1 
ATOM   785  N N   . PRO A 1 101 ? 36.682  -39.428 -15.649 1.00 21.47 ? 102 PRO A N   1 
ATOM   786  C CA  . PRO A 1 101 ? 37.007  -39.650 -14.231 1.00 21.91 ? 102 PRO A CA  1 
ATOM   787  C C   . PRO A 1 101 ? 35.964  -39.144 -13.257 1.00 22.04 ? 102 PRO A C   1 
ATOM   788  O O   . PRO A 1 101 ? 35.825  -39.748 -12.186 1.00 20.39 ? 102 PRO A O   1 
ATOM   789  C CB  . PRO A 1 101 ? 38.331  -38.900 -14.052 1.00 20.23 ? 102 PRO A CB  1 
ATOM   790  C CG  . PRO A 1 101 ? 38.943  -38.895 -15.417 1.00 22.80 ? 102 PRO A CG  1 
ATOM   791  C CD  . PRO A 1 101 ? 37.776  -38.742 -16.360 1.00 23.33 ? 102 PRO A CD  1 
ATOM   792  N N   . ILE A 1 102 ? 35.242  -38.053 -13.560 1.00 19.48 ? 103 ILE A N   1 
ATOM   793  C CA  . ILE A 1 102 ? 34.244  -37.571 -12.595 1.00 19.30 ? 103 ILE A CA  1 
ATOM   794  C C   . ILE A 1 102 ? 33.104  -38.580 -12.434 1.00 21.71 ? 103 ILE A C   1 
ATOM   795  O O   . ILE A 1 102 ? 32.407  -38.585 -11.407 1.00 18.30 ? 103 ILE A O   1 
ATOM   796  C CB  . ILE A 1 102 ? 33.733  -36.158 -12.986 1.00 17.57 ? 103 ILE A CB  1 
ATOM   797  C CG1 . ILE A 1 102 ? 32.885  -35.553 -11.866 1.00 19.48 ? 103 ILE A CG1 1 
ATOM   798  C CG2 . ILE A 1 102 ? 32.886  -36.205 -14.246 1.00 22.16 ? 103 ILE A CG2 1 
ATOM   799  C CD1 . ILE A 1 102 ? 33.669  -35.064 -10.677 1.00 19.95 ? 103 ILE A CD1 1 
ATOM   800  N N   . ASP A 1 103 ? 32.930  -39.478 -13.398 1.00 19.65 ? 104 ASP A N   1 
ATOM   801  C CA  . ASP A 1 103 ? 31.908  -40.514 -13.287 1.00 21.69 ? 104 ASP A CA  1 
ATOM   802  C C   . ASP A 1 103 ? 32.289  -41.595 -12.295 1.00 23.10 ? 104 ASP A C   1 
ATOM   803  O O   . ASP A 1 103 ? 31.571  -42.587 -12.196 1.00 24.60 ? 104 ASP A O   1 
ATOM   804  C CB  . ASP A 1 103 ? 31.632  -41.138 -14.666 1.00 21.24 ? 104 ASP A CB  1 
ATOM   805  C CG  . ASP A 1 103 ? 30.243  -41.756 -14.765 1.00 25.30 ? 104 ASP A CG  1 
ATOM   806  O OD1 . ASP A 1 103 ? 29.369  -41.376 -13.976 1.00 24.65 ? 104 ASP A OD1 1 
ATOM   807  O OD2 . ASP A 1 103 ? 30.028  -42.656 -15.605 1.00 28.04 ? 104 ASP A OD2 1 
ATOM   808  N N   . GLN A 1 104 ? 33.414  -41.445 -11.588 1.00 20.18 ? 105 GLN A N   1 
ATOM   809  C CA  . GLN A 1 104 ? 33.787  -42.329 -10.492 1.00 19.41 ? 105 GLN A CA  1 
ATOM   810  C C   . GLN A 1 104 ? 33.350  -41.796 -9.129  1.00 19.41 ? 105 GLN A C   1 
ATOM   811  O O   . GLN A 1 104 ? 33.513  -42.506 -8.130  1.00 19.28 ? 105 GLN A O   1 
ATOM   812  C CB  . GLN A 1 104 ? 35.316  -42.560 -10.516 1.00 21.26 ? 105 GLN A CB  1 
ATOM   813  C CG  . GLN A 1 104 ? 35.787  -43.299 -11.785 1.00 23.39 ? 105 GLN A CG  1 
ATOM   814  C CD  . GLN A 1 104 ? 37.293  -43.215 -12.049 1.00 24.13 ? 105 GLN A CD  1 
ATOM   815  O OE1 . GLN A 1 104 ? 37.918  -42.159 -11.887 1.00 26.46 ? 105 GLN A OE1 1 
ATOM   816  N NE2 . GLN A 1 104 ? 37.870  -44.323 -12.509 1.00 26.32 ? 105 GLN A NE2 1 
ATOM   817  N N   . VAL A 1 105 ? 32.839  -40.553 -9.065  1.00 16.83 ? 106 VAL A N   1 
ATOM   818  C CA  . VAL A 1 105 ? 32.325  -39.946 -7.838  1.00 15.92 ? 106 VAL A CA  1 
ATOM   819  C C   . VAL A 1 105 ? 30.815  -40.161 -7.798  1.00 16.78 ? 106 VAL A C   1 
ATOM   820  O O   . VAL A 1 105 ? 30.137  -39.937 -8.805  1.00 18.39 ? 106 VAL A O   1 
ATOM   821  C CB  . VAL A 1 105 ? 32.663  -38.442 -7.797  1.00 16.23 ? 106 VAL A CB  1 
ATOM   822  C CG1 . VAL A 1 105 ? 32.274  -37.814 -6.446  1.00 15.18 ? 106 VAL A CG1 1 
ATOM   823  C CG2 . VAL A 1 105 ? 34.150  -38.212 -8.093  1.00 15.92 ? 106 VAL A CG2 1 
ATOM   824  N N   . ASN A 1 106 ? 30.272  -40.565 -6.643  1.00 16.07 ? 107 ASN A N   1 
ATOM   825  C CA  . ASN A 1 106 ? 28.822  -40.761 -6.592  1.00 16.77 ? 107 ASN A CA  1 
ATOM   826  C C   . ASN A 1 106 ? 28.073  -39.500 -6.122  1.00 18.30 ? 107 ASN A C   1 
ATOM   827  O O   . ASN A 1 106 ? 28.655  -38.478 -5.739  1.00 18.04 ? 107 ASN A O   1 
ATOM   828  C CB  . ASN A 1 106 ? 28.458  -42.019 -5.753  1.00 16.56 ? 107 ASN A CB  1 
ATOM   829  C CG  . ASN A 1 106 ? 28.685  -41.861 -4.252  1.00 18.95 ? 107 ASN A CG  1 
ATOM   830  O OD1 . ASN A 1 106 ? 28.524  -40.773 -3.671  1.00 20.00 ? 107 ASN A OD1 1 
ATOM   831  N ND2 . ASN A 1 106 ? 29.013  -42.974 -3.603  1.00 19.79 ? 107 ASN A ND2 1 
ATOM   832  N N   . LEU A 1 107 ? 26.738  -39.561 -6.204  1.00 16.56 ? 108 LEU A N   1 
ATOM   833  C CA  . LEU A 1 107 ? 25.939  -38.355 -5.996  1.00 17.15 ? 108 LEU A CA  1 
ATOM   834  C C   . LEU A 1 107 ? 25.998  -37.854 -4.552  1.00 14.61 ? 108 LEU A C   1 
ATOM   835  O O   . LEU A 1 107 ? 25.998  -36.642 -4.313  1.00 14.22 ? 108 LEU A O   1 
ATOM   836  C CB  . LEU A 1 107 ? 24.487  -38.631 -6.403  1.00 16.22 ? 108 LEU A CB  1 
ATOM   837  C CG  . LEU A 1 107 ? 24.271  -39.113 -7.843  1.00 19.49 ? 108 LEU A CG  1 
ATOM   838  C CD1 . LEU A 1 107 ? 22.758  -39.121 -8.148  1.00 16.83 ? 108 LEU A CD1 1 
ATOM   839  C CD2 . LEU A 1 107 ? 25.029  -38.273 -8.893  1.00 18.01 ? 108 LEU A CD2 1 
ATOM   840  N N   . LEU A 1 108 ? 26.005  -38.755 -3.575  1.00 16.47 ? 109 LEU A N   1 
ATOM   841  C CA  . LEU A 1 108 ? 26.095  -38.315 -2.186  1.00 17.33 ? 109 LEU A CA  1 
ATOM   842  C C   . LEU A 1 108 ? 27.418  -37.609 -1.929  1.00 17.67 ? 109 LEU A C   1 
ATOM   843  O O   . LEU A 1 108 ? 27.469  -36.604 -1.206  1.00 16.91 ? 109 LEU A O   1 
ATOM   844  C CB  . LEU A 1 108 ? 25.931  -39.513 -1.243  1.00 19.20 ? 109 LEU A CB  1 
ATOM   845  C CG  . LEU A 1 108 ? 25.985  -39.236 0.258   1.00 24.16 ? 109 LEU A CG  1 
ATOM   846  C CD1 . LEU A 1 108 ? 24.860  -38.302 0.710   1.00 22.81 ? 109 LEU A CD1 1 
ATOM   847  C CD2 . LEU A 1 108 ? 25.960  -40.575 1.049   1.00 24.89 ? 109 LEU A CD2 1 
ATOM   848  N N   . GLN A 1 109 ? 28.491  -38.099 -2.552  1.00 17.74 ? 110 GLN A N   1 
ATOM   849  C CA  . GLN A 1 109 ? 29.803  -37.465 -2.413  1.00 18.55 ? 110 GLN A CA  1 
ATOM   850  C C   . GLN A 1 109 ? 29.826  -36.082 -3.056  1.00 18.11 ? 110 GLN A C   1 
ATOM   851  O O   . GLN A 1 109 ? 30.448  -35.151 -2.520  1.00 18.68 ? 110 GLN A O   1 
ATOM   852  C CB  . GLN A 1 109 ? 30.883  -38.370 -3.017  1.00 15.31 ? 110 GLN A CB  1 
ATOM   853  C CG  . GLN A 1 109 ? 31.086  -39.687 -2.224  1.00 16.34 ? 110 GLN A CG  1 
ATOM   854  C CD  . GLN A 1 109 ? 31.876  -40.769 -2.979  1.00 19.03 ? 110 GLN A CD  1 
ATOM   855  O OE1 . GLN A 1 109 ? 31.937  -40.777 -4.210  1.00 18.88 ? 110 GLN A OE1 1 
ATOM   856  N NE2 . GLN A 1 109 ? 32.466  -41.709 -2.226  1.00 17.93 ? 110 GLN A NE2 1 
ATOM   857  N N   . LEU A 1 110 ? 29.135  -35.910 -4.189  1.00 16.54 ? 111 LEU A N   1 
ATOM   858  C CA  . LEU A 1 110 ? 29.002  -34.558 -4.743  1.00 13.98 ? 111 LEU A CA  1 
ATOM   859  C C   . LEU A 1 110 ? 28.201  -33.665 -3.808  1.00 16.69 ? 111 LEU A C   1 
ATOM   860  O O   . LEU A 1 110 ? 28.587  -32.517 -3.552  1.00 17.19 ? 111 LEU A O   1 
ATOM   861  C CB  . LEU A 1 110 ? 28.344  -34.611 -6.125  1.00 14.07 ? 111 LEU A CB  1 
ATOM   862  C CG  . LEU A 1 110 ? 29.172  -35.296 -7.229  1.00 19.86 ? 111 LEU A CG  1 
ATOM   863  C CD1 . LEU A 1 110 ? 28.355  -35.471 -8.531  1.00 19.18 ? 111 LEU A CD1 1 
ATOM   864  C CD2 . LEU A 1 110 ? 30.421  -34.489 -7.490  1.00 20.18 ? 111 LEU A CD2 1 
ATOM   865  N N   . ALA A 1 111 ? 27.059  -34.165 -3.314  1.00 17.25 ? 112 ALA A N   1 
ATOM   866  C CA  . ALA A 1 111 ? 26.186  -33.349 -2.479  1.00 15.81 ? 112 ALA A CA  1 
ATOM   867  C C   . ALA A 1 111 ? 26.847  -32.953 -1.166  1.00 19.16 ? 112 ALA A C   1 
ATOM   868  O O   . ALA A 1 111 ? 26.519  -31.892 -0.611  1.00 20.39 ? 112 ALA A O   1 
ATOM   869  C CB  . ALA A 1 111 ? 24.877  -34.089 -2.205  1.00 14.89 ? 112 ALA A CB  1 
ATOM   870  N N   . THR A 1 112 ? 27.806  -33.749 -0.677  1.00 17.12 ? 113 THR A N   1 
ATOM   871  C CA  . THR A 1 112 ? 28.435  -33.488 0.615   1.00 15.72 ? 113 THR A CA  1 
ATOM   872  C C   . THR A 1 112 ? 29.921  -33.158 0.489   1.00 17.19 ? 113 THR A C   1 
ATOM   873  O O   . THR A 1 112 ? 30.663  -33.247 1.486   1.00 16.32 ? 113 THR A O   1 
ATOM   874  C CB  . THR A 1 112 ? 28.211  -34.675 1.564   1.00 15.69 ? 113 THR A CB  1 
ATOM   875  O OG1 . THR A 1 112 ? 28.790  -35.857 1.006   1.00 18.47 ? 113 THR A OG1 1 
ATOM   876  C CG2 . THR A 1 112 ? 26.702  -34.918 1.774   1.00 17.21 ? 113 THR A CG2 1 
ATOM   877  N N   . TYR A 1 113 ? 30.359  -32.740 -0.707  1.00 17.58 ? 114 TYR A N   1 
ATOM   878  C CA  . TYR A 1 113 ? 31.641  -32.045 -0.920  1.00 17.97 ? 114 TYR A CA  1 
ATOM   879  C C   . TYR A 1 113 ? 32.858  -32.940 -0.701  1.00 16.37 ? 114 TYR A C   1 
ATOM   880  O O   . TYR A 1 113 ? 33.892  -32.461 -0.220  1.00 17.60 ? 114 TYR A O   1 
ATOM   881  C CB  . TYR A 1 113 ? 31.784  -30.792 -0.035  1.00 19.34 ? 114 TYR A CB  1 
ATOM   882  C CG  . TYR A 1 113 ? 30.518  -30.010 0.210   1.00 21.71 ? 114 TYR A CG  1 
ATOM   883  C CD1 . TYR A 1 113 ? 29.919  -29.265 -0.820  1.00 20.03 ? 114 TYR A CD1 1 
ATOM   884  C CD2 . TYR A 1 113 ? 29.932  -29.986 1.474   1.00 20.74 ? 114 TYR A CD2 1 
ATOM   885  C CE1 . TYR A 1 113 ? 28.739  -28.545 -0.590  1.00 20.67 ? 114 TYR A CE1 1 
ATOM   886  C CE2 . TYR A 1 113 ? 28.754  -29.266 1.706   1.00 20.48 ? 114 TYR A CE2 1 
ATOM   887  C CZ  . TYR A 1 113 ? 28.174  -28.555 0.671   1.00 22.99 ? 114 TYR A CZ  1 
ATOM   888  O OH  . TYR A 1 113 ? 27.021  -27.851 0.918   1.00 25.12 ? 114 TYR A OH  1 
ATOM   889  N N   . THR A 1 114 ? 32.786  -34.230 -1.069  1.00 18.28 ? 115 THR A N   1 
ATOM   890  C CA  . THR A 1 114 ? 33.926  -35.117 -0.819  1.00 18.95 ? 115 THR A CA  1 
ATOM   891  C C   . THR A 1 114 ? 34.533  -35.709 -2.100  1.00 20.25 ? 115 THR A C   1 
ATOM   892  O O   . THR A 1 114 ? 35.166  -36.768 -2.048  1.00 19.97 ? 115 THR A O   1 
ATOM   893  C CB  . THR A 1 114 ? 33.558  -36.259 0.147   1.00 22.21 ? 115 THR A CB  1 
ATOM   894  O OG1 . THR A 1 114 ? 32.568  -37.119 -0.444  1.00 19.81 ? 115 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 114 ? 33.081  -35.720 1.529   1.00 18.46 ? 115 THR A CG2 1 
ATOM   896  N N   . SER A 1 115 ? 34.399  -35.025 -3.246  1.00 17.37 ? 116 SER A N   1 
ATOM   897  C CA  . SER A 1 115 ? 34.964  -35.552 -4.486  1.00 16.59 ? 116 SER A CA  1 
ATOM   898  C C   . SER A 1 115 ? 36.479  -35.668 -4.415  1.00 19.06 ? 116 SER A C   1 
ATOM   899  O O   . SER A 1 115 ? 37.062  -36.471 -5.155  1.00 18.36 ? 116 SER A O   1 
ATOM   900  C CB  . SER A 1 115 ? 34.599  -34.670 -5.697  1.00 17.43 ? 116 SER A CB  1 
ATOM   901  O OG  . SER A 1 115 ? 35.328  -33.448 -5.680  1.00 18.77 ? 116 SER A OG  1 
ATOM   902  N N   . GLY A 1 116 ? 37.126  -34.890 -3.547  1.00 18.48 ? 117 GLY A N   1 
ATOM   903  C CA  . GLY A 1 116 ? 38.572  -34.880 -3.443  1.00 19.01 ? 117 GLY A CA  1 
ATOM   904  C C   . GLY A 1 116 ? 39.296  -33.924 -4.378  1.00 18.09 ? 117 GLY A C   1 
ATOM   905  O O   . GLY A 1 116 ? 40.529  -33.812 -4.288  1.00 17.68 ? 117 GLY A O   1 
ATOM   906  N N   . ASN A 1 117 ? 38.592  -33.263 -5.298  1.00 16.88 ? 118 ASN A N   1 
ATOM   907  C CA  . ASN A 1 117 ? 39.257  -32.243 -6.110  1.00 21.06 ? 118 ASN A CA  1 
ATOM   908  C C   . ASN A 1 117 ? 38.280  -31.194 -6.647  1.00 19.20 ? 118 ASN A C   1 
ATOM   909  O O   . ASN A 1 117 ? 38.271  -30.912 -7.852  1.00 18.83 ? 118 ASN A O   1 
ATOM   910  C CB  . ASN A 1 117 ? 40.031  -32.883 -7.278  1.00 18.13 ? 118 ASN A CB  1 
ATOM   911  C CG  . ASN A 1 117 ? 41.018  -31.901 -7.931  1.00 21.10 ? 118 ASN A CG  1 
ATOM   912  O OD1 . ASN A 1 117 ? 41.454  -30.939 -7.297  1.00 20.72 ? 118 ASN A OD1 1 
ATOM   913  N ND2 . ASN A 1 117 ? 41.353  -32.136 -9.204  1.00 18.05 ? 118 ASN A ND2 1 
ATOM   914  N N   . LEU A 1 118 ? 37.455  -30.601 -5.784  1.00 20.16 ? 119 LEU A N   1 
ATOM   915  C CA  . LEU A 1 118 ? 36.617  -29.472 -6.196  1.00 18.08 ? 119 LEU A CA  1 
ATOM   916  C C   . LEU A 1 118 ? 36.688  -28.386 -5.138  1.00 18.32 ? 119 LEU A C   1 
ATOM   917  O O   . LEU A 1 118 ? 36.398  -28.639 -3.963  1.00 17.35 ? 119 LEU A O   1 
ATOM   918  C CB  . LEU A 1 118 ? 35.153  -29.879 -6.424  1.00 17.97 ? 119 LEU A CB  1 
ATOM   919  C CG  . LEU A 1 118 ? 34.899  -30.794 -7.640  1.00 20.78 ? 119 LEU A CG  1 
ATOM   920  C CD1 . LEU A 1 118 ? 33.446  -31.284 -7.668  1.00 19.05 ? 119 LEU A CD1 1 
ATOM   921  C CD2 . LEU A 1 118 ? 35.246  -30.049 -8.939  1.00 17.08 ? 119 LEU A CD2 1 
ATOM   922  N N   . ALA A 1 119 ? 37.039  -27.180 -5.566  1.00 18.33 ? 120 ALA A N   1 
ATOM   923  C CA  . ALA A 1 119 ? 37.271  -26.062 -4.663  1.00 21.58 ? 120 ALA A CA  1 
ATOM   924  C C   . ALA A 1 119 ? 35.993  -25.252 -4.453  1.00 19.64 ? 120 ALA A C   1 
ATOM   925  O O   . ALA A 1 119 ? 34.920  -25.595 -4.949  1.00 19.36 ? 120 ALA A O   1 
ATOM   926  C CB  . ALA A 1 119 ? 38.389  -25.171 -5.203  1.00 23.56 ? 120 ALA A CB  1 
ATOM   927  N N   . LEU A 1 120 ? 36.111  -24.141 -3.712  1.00 19.47 ? 121 LEU A N   1 
ATOM   928  C CA  . LEU A 1 120 ? 34.925  -23.354 -3.385  1.00 23.42 ? 121 LEU A CA  1 
ATOM   929  C C   . LEU A 1 120 ? 34.210  -22.862 -4.643  1.00 21.13 ? 121 LEU A C   1 
ATOM   930  O O   . LEU A 1 120 ? 32.971  -22.898 -4.715  1.00 19.94 ? 121 LEU A O   1 
ATOM   931  C CB  . LEU A 1 120 ? 35.309  -22.167 -2.497  1.00 20.79 ? 121 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 120 ? 34.117  -21.301 -2.082  1.00 24.55 ? 121 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 120 ? 33.112  -22.132 -1.283  1.00 27.28 ? 121 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 120 ? 34.573  -20.065 -1.273  1.00 28.51 ? 121 LEU A CD2 1 
ATOM   935  N N   . GLN A 1 121 ? 34.965  -22.384 -5.634  1.00 21.71 ? 122 GLN A N   1 
ATOM   936  C CA  . GLN A 1 121 ? 34.394  -21.857 -6.871  1.00 21.84 ? 122 GLN A CA  1 
ATOM   937  C C   . GLN A 1 121 ? 35.002  -22.556 -8.083  1.00 21.57 ? 122 GLN A C   1 
ATOM   938  O O   . GLN A 1 121 ? 36.089  -23.134 -8.011  1.00 21.45 ? 122 GLN A O   1 
ATOM   939  C CB  . GLN A 1 121 ? 34.628  -20.347 -7.009  1.00 21.25 ? 122 GLN A CB  1 
ATOM   940  C CG  . GLN A 1 121 ? 34.288  -19.522 -5.752  1.00 20.55 ? 122 GLN A CG  1 
ATOM   941  C CD  . GLN A 1 121 ? 32.798  -19.406 -5.502  1.00 25.09 ? 122 GLN A CD  1 
ATOM   942  O OE1 . GLN A 1 121 ? 31.981  -19.914 -6.274  1.00 25.32 ? 122 GLN A OE1 1 
ATOM   943  N NE2 . GLN A 1 121 ? 32.430  -18.727 -4.411  1.00 28.07 ? 122 GLN A NE2 1 
ATOM   944  N N   . PHE A 1 122 ? 34.293  -22.469 -9.217  1.00 21.60 ? 123 PHE A N   1 
ATOM   945  C CA  . PHE A 1 122 ? 34.893  -22.820 -10.502 1.00 24.54 ? 123 PHE A CA  1 
ATOM   946  C C   . PHE A 1 122 ? 36.118  -21.944 -10.743 1.00 22.80 ? 123 PHE A C   1 
ATOM   947  O O   . PHE A 1 122 ? 36.202  -20.821 -10.227 1.00 23.97 ? 123 PHE A O   1 
ATOM   948  C CB  . PHE A 1 122 ? 33.910  -22.604 -11.665 1.00 22.69 ? 123 PHE A CB  1 
ATOM   949  C CG  . PHE A 1 122 ? 32.821  -23.630 -11.757 1.00 22.65 ? 123 PHE A CG  1 
ATOM   950  C CD1 . PHE A 1 122 ? 33.112  -24.939 -12.151 1.00 22.39 ? 123 PHE A CD1 1 
ATOM   951  C CD2 . PHE A 1 122 ? 31.505  -23.292 -11.471 1.00 22.32 ? 123 PHE A CD2 1 
ATOM   952  C CE1 . PHE A 1 122 ? 32.108  -25.897 -12.242 1.00 23.25 ? 123 PHE A CE1 1 
ATOM   953  C CE2 . PHE A 1 122 ? 30.486  -24.239 -11.553 1.00 23.17 ? 123 PHE A CE2 1 
ATOM   954  C CZ  . PHE A 1 122 ? 30.784  -25.552 -11.941 1.00 21.65 ? 123 PHE A CZ  1 
ATOM   955  N N   . PRO A 1 123 ? 37.064  -22.412 -11.556 1.00 25.34 ? 124 PRO A N   1 
ATOM   956  C CA  . PRO A 1 123 ? 38.126  -21.516 -12.028 1.00 30.18 ? 124 PRO A CA  1 
ATOM   957  C C   . PRO A 1 123 ? 37.520  -20.291 -12.704 1.00 33.60 ? 124 PRO A C   1 
ATOM   958  O O   . PRO A 1 123 ? 36.408  -20.342 -13.236 1.00 29.08 ? 124 PRO A O   1 
ATOM   959  C CB  . PRO A 1 123 ? 38.910  -22.379 -13.025 1.00 31.14 ? 124 PRO A CB  1 
ATOM   960  C CG  . PRO A 1 123 ? 38.558  -23.789 -12.699 1.00 30.82 ? 124 PRO A CG  1 
ATOM   961  C CD  . PRO A 1 123 ? 37.160  -23.763 -12.142 1.00 25.25 ? 124 PRO A CD  1 
ATOM   962  N N   . ASP A 1 124 ? 38.262  -19.176 -12.668 1.00 31.80 ? 125 ASP A N   1 
ATOM   963  C CA  . ASP A 1 124 ? 37.747  -17.913 -13.201 1.00 34.86 ? 125 ASP A CA  1 
ATOM   964  C C   . ASP A 1 124 ? 37.383  -18.021 -14.677 1.00 35.02 ? 125 ASP A C   1 
ATOM   965  O O   . ASP A 1 124 ? 36.466  -17.339 -15.142 1.00 37.86 ? 125 ASP A O   1 
ATOM   966  C CB  . ASP A 1 124 ? 38.775  -16.795 -13.017 1.00 37.26 ? 125 ASP A CB  1 
ATOM   967  C CG  . ASP A 1 124 ? 38.804  -16.231 -11.603 1.00 42.94 ? 125 ASP A CG  1 
ATOM   968  O OD1 . ASP A 1 124 ? 38.073  -16.723 -10.718 1.00 39.65 ? 125 ASP A OD1 1 
ATOM   969  O OD2 . ASP A 1 124 ? 39.569  -15.265 -11.380 1.00 46.95 ? 125 ASP A OD2 1 
ATOM   970  N N   . GLU A 1 125 ? 38.093  -18.862 -15.427 1.00 36.80 ? 126 GLU A N   1 
ATOM   971  C CA  . GLU A 1 125 ? 37.874  -19.004 -16.862 1.00 39.30 ? 126 GLU A CA  1 
ATOM   972  C C   . GLU A 1 125 ? 36.593  -19.758 -17.208 1.00 35.38 ? 126 GLU A C   1 
ATOM   973  O O   . GLU A 1 125 ? 36.170  -19.708 -18.370 1.00 34.47 ? 126 GLU A O   1 
ATOM   974  C CB  . GLU A 1 125 ? 39.084  -19.706 -17.497 1.00 42.00 ? 126 GLU A CB  1 
ATOM   975  C CG  . GLU A 1 125 ? 39.644  -20.882 -16.664 1.00 47.96 ? 126 GLU A CG  1 
ATOM   976  C CD  . GLU A 1 125 ? 40.556  -20.433 -15.510 1.00 53.22 ? 126 GLU A CD  1 
ATOM   977  O OE1 . GLU A 1 125 ? 41.454  -21.207 -15.116 1.00 58.31 ? 126 GLU A OE1 1 
ATOM   978  O OE2 . GLU A 1 125 ? 40.370  -19.308 -14.995 1.00 57.97 ? 126 GLU A OE2 1 
ATOM   979  N N   . VAL A 1 126 ? 35.964  -20.441 -16.248 1.00 31.53 ? 127 VAL A N   1 
ATOM   980  C CA  . VAL A 1 126 ? 34.758  -21.224 -16.506 1.00 29.93 ? 127 VAL A CA  1 
ATOM   981  C C   . VAL A 1 126 ? 33.554  -20.309 -16.308 1.00 30.49 ? 127 VAL A C   1 
ATOM   982  O O   . VAL A 1 126 ? 33.123  -20.063 -15.181 1.00 28.32 ? 127 VAL A O   1 
ATOM   983  C CB  . VAL A 1 126 ? 34.685  -22.457 -15.608 1.00 26.07 ? 127 VAL A CB  1 
ATOM   984  C CG1 . VAL A 1 126 ? 33.375  -23.183 -15.836 1.00 27.57 ? 127 VAL A CG1 1 
ATOM   985  C CG2 . VAL A 1 126 ? 35.848  -23.363 -15.894 1.00 27.04 ? 127 VAL A CG2 1 
ATOM   986  N N   . LYS A 1 127 ? 32.990  -19.816 -17.416 1.00 29.50 ? 128 LYS A N   1 
ATOM   987  C CA  . LYS A 1 127 ? 31.961  -18.789 -17.358 1.00 27.94 ? 128 LYS A CA  1 
ATOM   988  C C   . LYS A 1 127 ? 30.637  -19.165 -18.007 1.00 30.72 ? 128 LYS A C   1 
ATOM   989  O O   . LYS A 1 127 ? 29.633  -18.512 -17.706 1.00 30.89 ? 128 LYS A O   1 
ATOM   990  C CB  . LYS A 1 127 ? 32.466  -17.491 -18.013 1.00 32.08 ? 128 LYS A CB  1 
ATOM   991  C CG  . LYS A 1 127 ? 33.661  -16.871 -17.306 1.00 35.05 ? 128 LYS A CG  1 
ATOM   992  C CD  . LYS A 1 127 ? 34.118  -15.596 -17.998 1.00 37.01 ? 128 LYS A CD  1 
ATOM   993  C CE  . LYS A 1 127 ? 35.421  -15.092 -17.402 1.00 40.03 ? 128 LYS A CE  1 
ATOM   994  N NZ  . LYS A 1 127 ? 35.242  -14.638 -15.996 1.00 40.42 ? 128 LYS A NZ  1 
ATOM   995  N N   . THR A 1 128 ? 30.599  -20.171 -18.890 1.00 24.56 ? 129 THR A N   1 
ATOM   996  C CA  . THR A 1 128 ? 29.398  -20.519 -19.640 1.00 24.81 ? 129 THR A CA  1 
ATOM   997  C C   . THR A 1 128 ? 29.019  -21.972 -19.376 1.00 26.47 ? 129 THR A C   1 
ATOM   998  O O   . THR A 1 128 ? 29.825  -22.757 -18.879 1.00 24.72 ? 129 THR A O   1 
ATOM   999  C CB  . THR A 1 128 ? 29.599  -20.321 -21.151 1.00 29.52 ? 129 THR A CB  1 
ATOM   1000 O OG1 . THR A 1 128 ? 30.431  -21.374 -21.657 1.00 26.49 ? 129 THR A OG1 1 
ATOM   1001 C CG2 . THR A 1 128 ? 30.255  -18.939 -21.468 1.00 26.53 ? 129 THR A CG2 1 
ATOM   1002 N N   . ASP A 1 129 ? 27.779  -22.328 -19.721 1.00 24.42 ? 130 ASP A N   1 
ATOM   1003 C CA  . ASP A 1 129 ? 27.340  -23.715 -19.565 1.00 26.85 ? 130 ASP A CA  1 
ATOM   1004 C C   . ASP A 1 129 ? 28.238  -24.682 -20.334 1.00 27.25 ? 130 ASP A C   1 
ATOM   1005 O O   . ASP A 1 129 ? 28.561  -25.768 -19.830 1.00 25.29 ? 130 ASP A O   1 
ATOM   1006 C CB  . ASP A 1 129 ? 25.891  -23.872 -20.032 1.00 29.29 ? 130 ASP A CB  1 
ATOM   1007 C CG  . ASP A 1 129 ? 24.891  -23.218 -19.090 1.00 36.95 ? 130 ASP A CG  1 
ATOM   1008 O OD1 . ASP A 1 129 ? 25.247  -22.962 -17.920 1.00 38.96 ? 130 ASP A OD1 1 
ATOM   1009 O OD2 . ASP A 1 129 ? 23.739  -22.977 -19.516 1.00 40.94 ? 130 ASP A OD2 1 
ATOM   1010 N N   . GLN A 1 130 ? 28.618  -24.324 -21.568 1.00 24.18 ? 131 GLN A N   1 
ATOM   1011 C CA  . GLN A 1 130 ? 29.521  -25.175 -22.352 1.00 25.90 ? 131 GLN A CA  1 
ATOM   1012 C C   . GLN A 1 130 ? 30.831  -25.405 -21.615 1.00 25.45 ? 131 GLN A C   1 
ATOM   1013 O O   . GLN A 1 130 ? 31.330  -26.538 -21.549 1.00 22.78 ? 131 GLN A O   1 
ATOM   1014 C CB  . GLN A 1 130 ? 29.814  -24.556 -23.718 1.00 28.76 ? 131 GLN A CB  1 
ATOM   1015 C CG  . GLN A 1 130 ? 28.649  -24.532 -24.675 1.00 27.94 ? 131 GLN A CG  1 
ATOM   1016 C CD  . GLN A 1 130 ? 29.043  -24.110 -26.081 1.00 30.10 ? 131 GLN A CD  1 
ATOM   1017 O OE1 . GLN A 1 130 ? 30.224  -24.114 -26.458 1.00 28.19 ? 131 GLN A OE1 1 
ATOM   1018 N NE2 . GLN A 1 130 ? 28.046  -23.758 -26.877 1.00 29.48 ? 131 GLN A NE2 1 
ATOM   1019 N N   . GLN A 1 131 ? 31.397  -24.341 -21.045 1.00 23.40 ? 132 GLN A N   1 
ATOM   1020 C CA  . GLN A 1 131 ? 32.684  -24.462 -20.367 1.00 24.31 ? 132 GLN A CA  1 
ATOM   1021 C C   . GLN A 1 131 ? 32.580  -25.292 -19.091 1.00 20.87 ? 132 GLN A C   1 
ATOM   1022 O O   . GLN A 1 131 ? 33.565  -25.935 -18.695 1.00 20.37 ? 132 GLN A O   1 
ATOM   1023 C CB  . GLN A 1 131 ? 33.246  -23.067 -20.093 1.00 23.77 ? 132 GLN A CB  1 
ATOM   1024 C CG  . GLN A 1 131 ? 33.548  -22.295 -21.404 1.00 23.42 ? 132 GLN A CG  1 
ATOM   1025 C CD  . GLN A 1 131 ? 33.661  -20.800 -21.222 1.00 30.32 ? 132 GLN A CD  1 
ATOM   1026 O OE1 . GLN A 1 131 ? 33.596  -20.289 -20.112 1.00 27.74 ? 132 GLN A OE1 1 
ATOM   1027 N NE2 . GLN A 1 131 ? 33.814  -20.090 -22.323 1.00 27.83 ? 132 GLN A NE2 1 
ATOM   1028 N N   . VAL A 1 132 ? 31.409  -25.309 -18.444 1.00 20.92 ? 133 VAL A N   1 
ATOM   1029 C CA  . VAL A 1 132 ? 31.227  -26.149 -17.256 1.00 20.26 ? 133 VAL A CA  1 
ATOM   1030 C C   . VAL A 1 132 ? 31.263  -27.620 -17.634 1.00 22.47 ? 133 VAL A C   1 
ATOM   1031 O O   . VAL A 1 132 ? 31.824  -28.449 -16.906 1.00 20.74 ? 133 VAL A O   1 
ATOM   1032 C CB  . VAL A 1 132 ? 29.914  -25.807 -16.521 1.00 21.12 ? 133 VAL A CB  1 
ATOM   1033 C CG1 . VAL A 1 132 ? 29.552  -26.916 -15.508 1.00 22.62 ? 133 VAL A CG1 1 
ATOM   1034 C CG2 . VAL A 1 132 ? 30.043  -24.484 -15.792 1.00 24.29 ? 133 VAL A CG2 1 
ATOM   1035 N N   . LEU A 1 133 ? 30.626  -27.980 -18.746 1.00 20.83 ? 134 LEU A N   1 
ATOM   1036 C CA  . LEU A 1 133 ? 30.687  -29.369 -19.193 1.00 19.65 ? 134 LEU A CA  1 
ATOM   1037 C C   . LEU A 1 133 ? 32.119  -29.757 -19.539 1.00 21.23 ? 134 LEU A C   1 
ATOM   1038 O O   . LEU A 1 133 ? 32.600  -30.831 -19.148 1.00 22.76 ? 134 LEU A O   1 
ATOM   1039 C CB  . LEU A 1 133 ? 29.760  -29.567 -20.392 1.00 19.99 ? 134 LEU A CB  1 
ATOM   1040 C CG  . LEU A 1 133 ? 29.781  -30.937 -21.082 1.00 22.80 ? 134 LEU A CG  1 
ATOM   1041 C CD1 . LEU A 1 133 ? 29.536  -32.038 -20.052 1.00 21.83 ? 134 LEU A CD1 1 
ATOM   1042 C CD2 . LEU A 1 133 ? 28.732  -30.969 -22.213 1.00 25.19 ? 134 LEU A CD2 1 
ATOM   1043 N N   . THR A 1 134 ? 32.814  -28.893 -20.284 1.00 20.34 ? 135 THR A N   1 
ATOM   1044 C CA  . THR A 1 134 ? 34.221  -29.146 -20.596 1.00 20.75 ? 135 THR A CA  1 
ATOM   1045 C C   . THR A 1 134 ? 35.042  -29.285 -19.315 1.00 21.59 ? 135 THR A C   1 
ATOM   1046 O O   . THR A 1 134 ? 35.880  -30.191 -19.195 1.00 21.73 ? 135 THR A O   1 
ATOM   1047 C CB  . THR A 1 134 ? 34.776  -28.022 -21.470 1.00 21.63 ? 135 THR A CB  1 
ATOM   1048 O OG1 . THR A 1 134 ? 34.110  -28.015 -22.747 1.00 22.41 ? 135 THR A OG1 1 
ATOM   1049 C CG2 . THR A 1 134 ? 36.301  -28.172 -21.678 1.00 22.10 ? 135 THR A CG2 1 
ATOM   1050 N N   . PHE A 1 135 ? 34.807  -28.397 -18.345 1.00 19.61 ? 136 PHE A N   1 
ATOM   1051 C CA  . PHE A 1 135 ? 35.480  -28.502 -17.049 1.00 19.64 ? 136 PHE A CA  1 
ATOM   1052 C C   . PHE A 1 135 ? 35.294  -29.884 -16.417 1.00 20.08 ? 136 PHE A C   1 
ATOM   1053 O O   . PHE A 1 135 ? 36.260  -30.505 -15.950 1.00 18.51 ? 136 PHE A O   1 
ATOM   1054 C CB  . PHE A 1 135 ? 34.963  -27.415 -16.105 1.00 21.27 ? 136 PHE A CB  1 
ATOM   1055 C CG  . PHE A 1 135 ? 35.485  -27.543 -14.696 1.00 18.30 ? 136 PHE A CG  1 
ATOM   1056 C CD1 . PHE A 1 135 ? 36.781  -27.130 -14.385 1.00 20.51 ? 136 PHE A CD1 1 
ATOM   1057 C CD2 . PHE A 1 135 ? 34.693  -28.090 -13.691 1.00 22.89 ? 136 PHE A CD2 1 
ATOM   1058 C CE1 . PHE A 1 135 ? 37.276  -27.245 -13.091 1.00 21.41 ? 136 PHE A CE1 1 
ATOM   1059 C CE2 . PHE A 1 135 ? 35.181  -28.219 -12.392 1.00 22.14 ? 136 PHE A CE2 1 
ATOM   1060 C CZ  . PHE A 1 135 ? 36.474  -27.802 -12.093 1.00 22.85 ? 136 PHE A CZ  1 
ATOM   1061 N N   . PHE A 1 136 ? 34.053  -30.380 -16.373 1.00 18.52 ? 137 PHE A N   1 
ATOM   1062 C CA  . PHE A 1 136 ? 33.828  -31.674 -15.728 1.00 18.88 ? 137 PHE A CA  1 
ATOM   1063 C C   . PHE A 1 136 ? 34.333  -32.841 -16.576 1.00 18.93 ? 137 PHE A C   1 
ATOM   1064 O O   . PHE A 1 136 ? 34.725  -33.871 -16.018 1.00 19.62 ? 137 PHE A O   1 
ATOM   1065 C CB  . PHE A 1 136 ? 32.342  -31.849 -15.376 1.00 19.96 ? 137 PHE A CB  1 
ATOM   1066 C CG  . PHE A 1 136 ? 31.919  -31.093 -14.121 1.00 19.26 ? 137 PHE A CG  1 
ATOM   1067 C CD1 . PHE A 1 136 ? 32.522  -31.361 -12.902 1.00 20.07 ? 137 PHE A CD1 1 
ATOM   1068 C CD2 . PHE A 1 136 ? 30.926  -30.120 -14.172 1.00 21.72 ? 137 PHE A CD2 1 
ATOM   1069 C CE1 . PHE A 1 136 ? 32.142  -30.661 -11.743 1.00 20.62 ? 137 PHE A CE1 1 
ATOM   1070 C CE2 . PHE A 1 136 ? 30.540  -29.424 -13.025 1.00 20.76 ? 137 PHE A CE2 1 
ATOM   1071 C CZ  . PHE A 1 136 ? 31.152  -29.701 -11.816 1.00 21.78 ? 137 PHE A CZ  1 
ATOM   1072 N N   . LYS A 1 137 ? 34.355  -32.719 -17.907 1.00 19.13 ? 138 LYS A N   1 
ATOM   1073 C CA  . LYS A 1 137 ? 34.910  -33.813 -18.706 1.00 21.43 ? 138 LYS A CA  1 
ATOM   1074 C C   . LYS A 1 137 ? 36.425  -33.917 -18.525 1.00 25.02 ? 138 LYS A C   1 
ATOM   1075 O O   . LYS A 1 137 ? 36.988  -35.022 -18.565 1.00 22.93 ? 138 LYS A O   1 
ATOM   1076 C CB  . LYS A 1 137 ? 34.573  -33.634 -20.192 1.00 23.85 ? 138 LYS A CB  1 
ATOM   1077 C CG  . LYS A 1 137 ? 33.104  -33.836 -20.527 1.00 21.99 ? 138 LYS A CG  1 
ATOM   1078 C CD  . LYS A 1 137 ? 32.897  -34.043 -22.038 1.00 30.07 ? 138 LYS A CD  1 
ATOM   1079 C CE  . LYS A 1 137 ? 33.521  -32.933 -22.874 1.00 31.05 ? 138 LYS A CE  1 
ATOM   1080 N NZ  . LYS A 1 137 ? 33.328  -33.150 -24.370 1.00 30.56 ? 138 LYS A NZ  1 
ATOM   1081 N N   . ASP A 1 138 ? 37.092  -32.783 -18.320 1.00 22.49 ? 139 ASP A N   1 
ATOM   1082 C CA  . ASP A 1 138 ? 38.541  -32.730 -18.159 1.00 23.24 ? 139 ASP A CA  1 
ATOM   1083 C C   . ASP A 1 138 ? 38.997  -32.993 -16.725 1.00 22.04 ? 139 ASP A C   1 
ATOM   1084 O O   . ASP A 1 138 ? 40.210  -33.092 -16.484 1.00 24.92 ? 139 ASP A O   1 
ATOM   1085 C CB  . ASP A 1 138 ? 39.067  -31.354 -18.602 1.00 25.53 ? 139 ASP A CB  1 
ATOM   1086 C CG  . ASP A 1 138 ? 38.924  -31.111 -20.111 1.00 30.82 ? 139 ASP A CG  1 
ATOM   1087 O OD1 . ASP A 1 138 ? 38.577  -32.056 -20.852 1.00 32.84 ? 139 ASP A OD1 1 
ATOM   1088 O OD2 . ASP A 1 138 ? 39.173  -29.962 -20.552 1.00 31.15 ? 139 ASP A OD2 1 
ATOM   1089 N N   . TRP A 1 139 ? 38.065  -33.079 -15.781 1.00 19.82 ? 140 TRP A N   1 
ATOM   1090 C CA  . TRP A 1 139 ? 38.391  -33.231 -14.359 1.00 21.52 ? 140 TRP A CA  1 
ATOM   1091 C C   . TRP A 1 139 ? 39.117  -34.546 -14.090 1.00 19.28 ? 140 TRP A C   1 
ATOM   1092 O O   . TRP A 1 139 ? 38.806  -35.585 -14.679 1.00 19.00 ? 140 TRP A O   1 
ATOM   1093 C CB  . TRP A 1 139 ? 37.098  -33.167 -13.543 1.00 19.68 ? 140 TRP A CB  1 
ATOM   1094 C CG  . TRP A 1 139 ? 37.216  -33.258 -12.056 1.00 19.86 ? 140 TRP A CG  1 
ATOM   1095 C CD1 . TRP A 1 139 ? 37.315  -32.211 -11.172 1.00 19.32 ? 140 TRP A CD1 1 
ATOM   1096 C CD2 . TRP A 1 139 ? 37.187  -34.452 -11.261 1.00 16.96 ? 140 TRP A CD2 1 
ATOM   1097 N NE1 . TRP A 1 139 ? 37.361  -32.691 -9.881  1.00 18.83 ? 140 TRP A NE1 1 
ATOM   1098 C CE2 . TRP A 1 139 ? 37.299  -34.061 -9.910  1.00 17.23 ? 140 TRP A CE2 1 
ATOM   1099 C CE3 . TRP A 1 139 ? 37.104  -35.816 -11.563 1.00 17.28 ? 140 TRP A CE3 1 
ATOM   1100 C CZ2 . TRP A 1 139 ? 37.326  -34.989 -8.855  1.00 16.57 ? 140 TRP A CZ2 1 
ATOM   1101 C CZ3 . TRP A 1 139 ? 37.115  -36.730 -10.519 1.00 17.16 ? 140 TRP A CZ3 1 
ATOM   1102 C CH2 . TRP A 1 139 ? 37.214  -36.306 -9.176  1.00 16.78 ? 140 TRP A CH2 1 
ATOM   1103 N N   . LYS A 1 140 ? 40.101  -34.492 -13.199 1.00 21.42 ? 141 LYS A N   1 
ATOM   1104 C CA  . LYS A 1 140 ? 40.797  -35.651 -12.660 1.00 18.80 ? 141 LYS A CA  1 
ATOM   1105 C C   . LYS A 1 140 ? 40.786  -35.592 -11.140 1.00 20.53 ? 141 LYS A C   1 
ATOM   1106 O O   . LYS A 1 140 ? 40.866  -34.502 -10.557 1.00 22.42 ? 141 LYS A O   1 
ATOM   1107 C CB  . LYS A 1 140 ? 42.250  -35.718 -13.157 1.00 19.82 ? 141 LYS A CB  1 
ATOM   1108 C CG  . LYS A 1 140 ? 42.363  -36.191 -14.616 1.00 26.83 ? 141 LYS A CG  1 
ATOM   1109 C CD  . LYS A 1 140 ? 43.764  -36.669 -14.934 1.00 25.31 ? 141 LYS A CD  1 
ATOM   1110 C CE  . LYS A 1 140 ? 43.815  -37.370 -16.273 1.00 31.25 ? 141 LYS A CE  1 
ATOM   1111 N NZ  . LYS A 1 140 ? 43.700  -36.410 -17.399 1.00 36.35 ? 141 LYS A NZ  1 
ATOM   1112 N N   . PRO A 1 141 ? 40.691  -36.743 -10.474 1.00 18.30 ? 142 PRO A N   1 
ATOM   1113 C CA  . PRO A 1 141 ? 40.690  -36.759 -9.008  1.00 18.01 ? 142 PRO A CA  1 
ATOM   1114 C C   . PRO A 1 141 ? 42.065  -36.416 -8.438  1.00 22.98 ? 142 PRO A C   1 
ATOM   1115 O O   . PRO A 1 141 ? 43.093  -36.529 -9.110  1.00 23.53 ? 142 PRO A O   1 
ATOM   1116 C CB  . PRO A 1 141 ? 40.299  -38.211 -8.666  1.00 18.81 ? 142 PRO A CB  1 
ATOM   1117 C CG  . PRO A 1 141 ? 40.713  -39.020 -9.857  1.00 18.66 ? 142 PRO A CG  1 
ATOM   1118 C CD  . PRO A 1 141 ? 40.540  -38.098 -11.058 1.00 19.20 ? 142 PRO A CD  1 
ATOM   1119 N N   . LYS A 1 142 ? 42.068  -35.985 -7.168  1.00 20.12 ? 143 LYS A N   1 
ATOM   1120 C CA  . LYS A 1 142 ? 43.321  -35.806 -6.429  1.00 21.84 ? 143 LYS A CA  1 
ATOM   1121 C C   . LYS A 1 142 ? 43.298  -36.621 -5.138  1.00 24.25 ? 143 LYS A C   1 
ATOM   1122 O O   . LYS A 1 142 ? 43.822  -37.741 -5.106  1.00 22.86 ? 143 LYS A O   1 
ATOM   1123 C CB  . LYS A 1 142 ? 43.591  -34.312 -6.149  1.00 21.68 ? 143 LYS A CB  1 
ATOM   1124 C CG  . LYS A 1 142 ? 44.367  -33.658 -7.281  1.00 27.36 ? 143 LYS A CG  1 
ATOM   1125 C CD  . LYS A 1 142 ? 44.771  -32.203 -6.997  1.00 27.87 ? 143 LYS A CD  1 
ATOM   1126 C CE  . LYS A 1 142 ? 45.679  -31.714 -8.132  1.00 29.85 ? 143 LYS A CE  1 
ATOM   1127 N NZ  . LYS A 1 142 ? 46.266  -30.365 -7.867  1.00 31.84 ? 143 LYS A NZ  1 
ATOM   1128 N N   . ASN A 1 143 ? 42.668  -36.094 -4.090  1.00 22.02 ? 144 ASN A N   1 
ATOM   1129 C CA  . ASN A 1 143 ? 42.529  -36.822 -2.833  1.00 22.15 ? 144 ASN A CA  1 
ATOM   1130 C C   . ASN A 1 143 ? 41.575  -38.009 -2.980  1.00 21.54 ? 144 ASN A C   1 
ATOM   1131 O O   . ASN A 1 143 ? 40.635  -37.975 -3.775  1.00 22.71 ? 144 ASN A O   1 
ATOM   1132 C CB  . ASN A 1 143 ? 42.013  -35.889 -1.740  1.00 22.36 ? 144 ASN A CB  1 
ATOM   1133 C CG  . ASN A 1 143 ? 42.794  -34.589 -1.666  1.00 23.83 ? 144 ASN A CG  1 
ATOM   1134 O OD1 . ASN A 1 143 ? 44.021  -34.575 -1.779  1.00 26.58 ? 144 ASN A OD1 1 
ATOM   1135 N ND2 . ASN A 1 143 ? 42.087  -33.497 -1.461  1.00 31.78 ? 144 ASN A ND2 1 
ATOM   1136 N N   . SER A 1 144 ? 41.810  -39.059 -2.180  1.00 20.53 ? 145 SER A N   1 
ATOM   1137 C CA  . SER A 1 144 ? 40.969  -40.253 -2.234  1.00 19.72 ? 145 SER A CA  1 
ATOM   1138 C C   . SER A 1 144 ? 39.496  -39.869 -2.239  1.00 20.44 ? 145 SER A C   1 
ATOM   1139 O O   . SER A 1 144 ? 39.031  -39.149 -1.351  1.00 18.75 ? 145 SER A O   1 
ATOM   1140 C CB  . SER A 1 144 ? 41.263  -41.168 -1.040  1.00 23.84 ? 145 SER A CB  1 
ATOM   1141 O OG  . SER A 1 144 ? 42.605  -41.590 -1.066  1.00 32.63 ? 145 SER A OG  1 
ATOM   1142 N N   . ILE A 1 145 ? 38.771  -40.325 -3.264  1.00 17.61 ? 146 ILE A N   1 
ATOM   1143 C CA  . ILE A 1 145 ? 37.359  -39.960 -3.401  1.00 20.48 ? 146 ILE A CA  1 
ATOM   1144 C C   . ILE A 1 145 ? 36.583  -40.379 -2.162  1.00 19.80 ? 146 ILE A C   1 
ATOM   1145 O O   . ILE A 1 145 ? 36.671  -41.529 -1.705  1.00 18.29 ? 146 ILE A O   1 
ATOM   1146 C CB  . ILE A 1 145 ? 36.770  -40.584 -4.675  1.00 19.52 ? 146 ILE A CB  1 
ATOM   1147 C CG1 . ILE A 1 145 ? 37.386  -39.929 -5.910  1.00 22.98 ? 146 ILE A CG1 1 
ATOM   1148 C CG2 . ILE A 1 145 ? 35.225  -40.486 -4.681  1.00 19.17 ? 146 ILE A CG2 1 
ATOM   1149 C CD1 . ILE A 1 145 ? 37.061  -40.636 -7.202  1.00 20.74 ? 146 ILE A CD1 1 
ATOM   1150 N N   . GLY A 1 146 ? 35.832  -39.432 -1.594  1.00 17.94 ? 147 GLY A N   1 
ATOM   1151 C CA  . GLY A 1 146 ? 34.982  -39.686 -0.448  1.00 20.75 ? 147 GLY A CA  1 
ATOM   1152 C C   . GLY A 1 146 ? 35.612  -39.411 0.905   1.00 20.62 ? 147 GLY A C   1 
ATOM   1153 O O   . GLY A 1 146 ? 34.897  -39.438 1.915   1.00 21.04 ? 147 GLY A O   1 
ATOM   1154 N N   . GLU A 1 147 ? 36.924  -39.150 0.968   1.00 17.80 ? 148 GLU A N   1 
ATOM   1155 C CA  . GLU A 1 147 ? 37.607  -39.113 2.259   1.00 18.97 ? 148 GLU A CA  1 
ATOM   1156 C C   . GLU A 1 147 ? 37.817  -37.709 2.825   1.00 19.18 ? 148 GLU A C   1 
ATOM   1157 O O   . GLU A 1 147 ? 38.051  -37.587 4.033   1.00 19.95 ? 148 GLU A O   1 
ATOM   1158 C CB  . GLU A 1 147 ? 38.964  -39.837 2.163   1.00 24.19 ? 148 GLU A CB  1 
ATOM   1159 C CG  . GLU A 1 147 ? 38.810  -41.347 1.855   1.00 26.56 ? 148 GLU A CG  1 
ATOM   1160 C CD  . GLU A 1 147 ? 40.081  -42.155 2.121   1.00 37.16 ? 148 GLU A CD  1 
ATOM   1161 O OE1 . GLU A 1 147 ? 40.056  -43.394 1.918   1.00 40.82 ? 148 GLU A OE1 1 
ATOM   1162 O OE2 . GLU A 1 147 ? 41.097  -41.558 2.562   1.00 40.88 ? 148 GLU A OE2 1 
ATOM   1163 N N   . TYR A 1 148 ? 37.740  -36.657 2.004   1.00 19.22 ? 149 TYR A N   1 
ATOM   1164 C CA  . TYR A 1 148 ? 38.014  -35.290 2.452   1.00 18.82 ? 149 TYR A CA  1 
ATOM   1165 C C   . TYR A 1 148 ? 36.906  -34.336 2.039   1.00 18.87 ? 149 TYR A C   1 
ATOM   1166 O O   . TYR A 1 148 ? 36.521  -34.298 0.864   1.00 20.02 ? 149 TYR A O   1 
ATOM   1167 C CB  . TYR A 1 148 ? 39.345  -34.783 1.893   1.00 21.15 ? 149 TYR A CB  1 
ATOM   1168 C CG  . TYR A 1 148 ? 40.490  -35.661 2.292   1.00 23.11 ? 149 TYR A CG  1 
ATOM   1169 C CD1 . TYR A 1 148 ? 40.806  -36.777 1.536   1.00 25.78 ? 149 TYR A CD1 1 
ATOM   1170 C CD2 . TYR A 1 148 ? 41.231  -35.408 3.439   1.00 26.97 ? 149 TYR A CD2 1 
ATOM   1171 C CE1 . TYR A 1 148 ? 41.838  -37.617 1.878   1.00 30.17 ? 149 TYR A CE1 1 
ATOM   1172 C CE2 . TYR A 1 148 ? 42.282  -36.272 3.806   1.00 25.57 ? 149 TYR A CE2 1 
ATOM   1173 C CZ  . TYR A 1 148 ? 42.571  -37.372 3.007   1.00 28.06 ? 149 TYR A CZ  1 
ATOM   1174 O OH  . TYR A 1 148 ? 43.619  -38.254 3.289   1.00 32.95 ? 149 TYR A OH  1 
ATOM   1175 N N   . ARG A 1 149 ? 36.463  -33.513 2.996   1.00 20.02 ? 150 ARG A N   1 
ATOM   1176 C CA  . ARG A 1 149 ? 35.467  -32.475 2.766   1.00 21.36 ? 150 ARG A CA  1 
ATOM   1177 C C   . ARG A 1 149 ? 36.142  -31.182 2.346   1.00 20.26 ? 150 ARG A C   1 
ATOM   1178 O O   . ARG A 1 149 ? 37.036  -30.685 3.045   1.00 20.94 ? 150 ARG A O   1 
ATOM   1179 C CB  . ARG A 1 149 ? 34.643  -32.217 4.032   1.00 17.53 ? 150 ARG A CB  1 
ATOM   1180 C CG  . ARG A 1 149 ? 33.585  -31.133 3.885   1.00 18.81 ? 150 ARG A CG  1 
ATOM   1181 C CD  . ARG A 1 149 ? 32.880  -30.890 5.224   1.00 17.51 ? 150 ARG A CD  1 
ATOM   1182 N NE  . ARG A 1 149 ? 31.666  -30.071 5.112   1.00 16.16 ? 150 ARG A NE  1 
ATOM   1183 C CZ  . ARG A 1 149 ? 31.676  -28.744 5.144   1.00 20.85 ? 150 ARG A CZ  1 
ATOM   1184 N NH1 . ARG A 1 149 ? 32.812  -28.061 5.177   1.00 18.09 ? 150 ARG A NH1 1 
ATOM   1185 N NH2 . ARG A 1 149 ? 30.521  -28.083 5.177   1.00 16.64 ? 150 ARG A NH2 1 
ATOM   1186 N N   . GLN A 1 150 ? 35.701  -30.618 1.226   1.00 18.34 ? 151 GLN A N   1 
ATOM   1187 C CA  . GLN A 1 150 ? 36.060  -29.237 0.885   1.00 20.37 ? 151 GLN A CA  1 
ATOM   1188 C C   . GLN A 1 150 ? 34.814  -28.546 0.356   1.00 19.48 ? 151 GLN A C   1 
ATOM   1189 O O   . GLN A 1 150 ? 34.326  -28.899 -0.722  1.00 18.59 ? 151 GLN A O   1 
ATOM   1190 C CB  . GLN A 1 150 ? 37.190  -29.176 -0.145  1.00 22.47 ? 151 GLN A CB  1 
ATOM   1191 C CG  . GLN A 1 150 ? 37.591  -27.737 -0.476  1.00 22.19 ? 151 GLN A CG  1 
ATOM   1192 C CD  . GLN A 1 150 ? 38.935  -27.656 -1.154  1.00 29.23 ? 151 GLN A CD  1 
ATOM   1193 O OE1 . GLN A 1 150 ? 39.263  -28.486 -2.001  1.00 28.71 ? 151 GLN A OE1 1 
ATOM   1194 N NE2 . GLN A 1 150 ? 39.727  -26.660 -0.783  1.00 32.03 ? 151 GLN A NE2 1 
ATOM   1195 N N   . TYR A 1 151 ? 34.298  -27.578 1.120   1.00 20.32 ? 152 TYR A N   1 
ATOM   1196 C CA  . TYR A 1 151 ? 33.079  -26.869 0.745   1.00 19.76 ? 152 TYR A CA  1 
ATOM   1197 C C   . TYR A 1 151 ? 33.217  -26.316 -0.670  1.00 17.72 ? 152 TYR A C   1 
ATOM   1198 O O   . TYR A 1 151 ? 34.249  -25.745 -1.013  1.00 19.52 ? 152 TYR A O   1 
ATOM   1199 C CB  . TYR A 1 151 ? 32.836  -25.736 1.747   1.00 21.98 ? 152 TYR A CB  1 
ATOM   1200 C CG  . TYR A 1 151 ? 31.497  -25.044 1.644   1.00 23.90 ? 152 TYR A CG  1 
ATOM   1201 C CD1 . TYR A 1 151 ? 30.324  -25.735 1.878   1.00 24.50 ? 152 TYR A CD1 1 
ATOM   1202 C CD2 . TYR A 1 151 ? 31.415  -23.687 1.353   1.00 29.09 ? 152 TYR A CD2 1 
ATOM   1203 C CE1 . TYR A 1 151 ? 29.095  -25.104 1.814   1.00 26.08 ? 152 TYR A CE1 1 
ATOM   1204 C CE2 . TYR A 1 151 ? 30.187  -23.044 1.279   1.00 31.02 ? 152 TYR A CE2 1 
ATOM   1205 C CZ  . TYR A 1 151 ? 29.034  -23.759 1.510   1.00 32.08 ? 152 TYR A CZ  1 
ATOM   1206 O OH  . TYR A 1 151 ? 27.813  -23.129 1.447   1.00 32.35 ? 152 TYR A OH  1 
ATOM   1207 N N   . SER A 1 152 ? 32.195  -26.521 -1.504  1.00 18.47 ? 153 SER A N   1 
ATOM   1208 C CA  . SER A 1 152 ? 32.402  -26.373 -2.948  1.00 18.97 ? 153 SER A CA  1 
ATOM   1209 C C   . SER A 1 152 ? 31.087  -26.115 -3.666  1.00 18.51 ? 153 SER A C   1 
ATOM   1210 O O   . SER A 1 152 ? 30.224  -26.989 -3.706  1.00 16.95 ? 153 SER A O   1 
ATOM   1211 C CB  . SER A 1 152 ? 33.067  -27.639 -3.516  1.00 18.62 ? 153 SER A CB  1 
ATOM   1212 O OG  . SER A 1 152 ? 33.025  -27.654 -4.943  1.00 18.16 ? 153 SER A OG  1 
ATOM   1213 N N   . ASN A 1 153 ? 30.975  -24.964 -4.315  1.00 14.94 ? 154 ASN A N   1 
ATOM   1214 C CA  . ASN A 1 153 ? 29.819  -24.646 -5.143  1.00 16.45 ? 154 ASN A CA  1 
ATOM   1215 C C   . ASN A 1 153 ? 29.750  -25.507 -6.413  1.00 17.58 ? 154 ASN A C   1 
ATOM   1216 O O   . ASN A 1 153 ? 28.656  -25.987 -6.762  1.00 18.07 ? 154 ASN A O   1 
ATOM   1217 C CB  . ASN A 1 153 ? 29.851  -23.143 -5.461  1.00 16.15 ? 154 ASN A CB  1 
ATOM   1218 C CG  . ASN A 1 153 ? 29.517  -22.300 -4.238  1.00 21.59 ? 154 ASN A CG  1 
ATOM   1219 O OD1 . ASN A 1 153 ? 28.558  -22.586 -3.528  1.00 21.08 ? 154 ASN A OD1 1 
ATOM   1220 N ND2 . ASN A 1 153 ? 30.297  -21.256 -3.994  1.00 26.58 ? 154 ASN A ND2 1 
ATOM   1221 N N   . PRO A 1 154 ? 30.861  -25.734 -7.133  1.00 18.05 ? 155 PRO A N   1 
ATOM   1222 C CA  . PRO A 1 154 ? 30.802  -26.687 -8.262  1.00 16.97 ? 155 PRO A CA  1 
ATOM   1223 C C   . PRO A 1 154 ? 30.297  -28.069 -7.869  1.00 17.00 ? 155 PRO A C   1 
ATOM   1224 O O   . PRO A 1 154 ? 29.549  -28.701 -8.641  1.00 19.84 ? 155 PRO A O   1 
ATOM   1225 C CB  . PRO A 1 154 ? 32.264  -26.739 -8.741  1.00 20.16 ? 155 PRO A CB  1 
ATOM   1226 C CG  . PRO A 1 154 ? 32.829  -25.411 -8.340  1.00 21.32 ? 155 PRO A CG  1 
ATOM   1227 C CD  . PRO A 1 154 ? 32.174  -25.054 -7.068  1.00 18.93 ? 155 PRO A CD  1 
ATOM   1228 N N   . SER A 1 155 ? 30.671  -28.550 -6.681  1.00 14.85 ? 156 SER A N   1 
ATOM   1229 C CA  . SER A 1 155 ? 30.277  -29.904 -6.260  1.00 14.41 ? 156 SER A CA  1 
ATOM   1230 C C   . SER A 1 155 ? 28.759  -30.009 -6.127  1.00 15.96 ? 156 SER A C   1 
ATOM   1231 O O   . SER A 1 155 ? 28.129  -30.886 -6.723  1.00 15.77 ? 156 SER A O   1 
ATOM   1232 C CB  . SER A 1 155 ? 30.961  -30.270 -4.935  1.00 14.19 ? 156 SER A CB  1 
ATOM   1233 O OG  . SER A 1 155 ? 30.879  -31.683 -4.659  1.00 16.14 ? 156 SER A OG  1 
ATOM   1234 N N   . ILE A 1 156 ? 28.142  -29.100 -5.372  1.00 18.64 ? 157 ILE A N   1 
ATOM   1235 C CA  . ILE A 1 156 ? 26.696  -29.240 -5.217  1.00 18.68 ? 157 ILE A CA  1 
ATOM   1236 C C   . ILE A 1 156 ? 25.947  -28.758 -6.457  1.00 17.61 ? 157 ILE A C   1 
ATOM   1237 O O   . ILE A 1 156 ? 24.797  -29.167 -6.679  1.00 20.27 ? 157 ILE A O   1 
ATOM   1238 C CB  . ILE A 1 156 ? 26.208  -28.538 -3.936  1.00 21.91 ? 157 ILE A CB  1 
ATOM   1239 C CG1 . ILE A 1 156 ? 24.752  -28.957 -3.622  1.00 23.47 ? 157 ILE A CG1 1 
ATOM   1240 C CG2 . ILE A 1 156 ? 26.334  -27.054 -4.076  1.00 21.61 ? 157 ILE A CG2 1 
ATOM   1241 C CD1 . ILE A 1 156 ? 24.401  -28.927 -2.141  1.00 23.24 ? 157 ILE A CD1 1 
ATOM   1242 N N   . GLY A 1 157 ? 26.556  -27.898 -7.279  1.00 18.51 ? 158 GLY A N   1 
ATOM   1243 C CA  . GLY A 1 157 ? 25.928  -27.527 -8.543  1.00 17.84 ? 158 GLY A CA  1 
ATOM   1244 C C   . GLY A 1 157 ? 25.765  -28.717 -9.476  1.00 19.75 ? 158 GLY A C   1 
ATOM   1245 O O   . GLY A 1 157 ? 24.718  -28.888 -10.105 1.00 19.67 ? 158 GLY A O   1 
ATOM   1246 N N   . LEU A 1 158 ? 26.802  -29.553 -9.581  1.00 17.56 ? 159 LEU A N   1 
ATOM   1247 C CA  . LEU A 1 158 ? 26.694  -30.774 -10.385 1.00 18.17 ? 159 LEU A CA  1 
ATOM   1248 C C   . LEU A 1 158 ? 25.637  -31.711 -9.806  1.00 19.03 ? 159 LEU A C   1 
ATOM   1249 O O   . LEU A 1 158 ? 24.834  -32.292 -10.546 1.00 19.10 ? 159 LEU A O   1 
ATOM   1250 C CB  . LEU A 1 158 ? 28.057  -31.482 -10.482 1.00 15.53 ? 159 LEU A CB  1 
ATOM   1251 C CG  . LEU A 1 158 ? 28.099  -32.799 -11.287 1.00 17.73 ? 159 LEU A CG  1 
ATOM   1252 C CD1 . LEU A 1 158 ? 27.542  -32.550 -12.687 1.00 20.60 ? 159 LEU A CD1 1 
ATOM   1253 C CD2 . LEU A 1 158 ? 29.533  -33.353 -11.373 1.00 18.41 ? 159 LEU A CD2 1 
ATOM   1254 N N   . PHE A 1 159 ? 25.611  -31.858 -8.480  1.00 16.64 ? 160 PHE A N   1 
ATOM   1255 C CA  . PHE A 1 159 ? 24.552  -32.646 -7.852  1.00 17.16 ? 160 PHE A CA  1 
ATOM   1256 C C   . PHE A 1 159 ? 23.175  -32.126 -8.256  1.00 18.71 ? 160 PHE A C   1 
ATOM   1257 O O   . PHE A 1 159 ? 22.306  -32.898 -8.670  1.00 17.86 ? 160 PHE A O   1 
ATOM   1258 C CB  . PHE A 1 159 ? 24.729  -32.637 -6.329  1.00 17.85 ? 160 PHE A CB  1 
ATOM   1259 C CG  . PHE A 1 159 ? 23.627  -33.328 -5.574  1.00 18.43 ? 160 PHE A CG  1 
ATOM   1260 C CD1 . PHE A 1 159 ? 23.558  -34.719 -5.535  1.00 17.05 ? 160 PHE A CD1 1 
ATOM   1261 C CD2 . PHE A 1 159 ? 22.667  -32.590 -4.887  1.00 17.73 ? 160 PHE A CD2 1 
ATOM   1262 C CE1 . PHE A 1 159 ? 22.551  -35.370 -4.838  1.00 19.43 ? 160 PHE A CE1 1 
ATOM   1263 C CE2 . PHE A 1 159 ? 21.661  -33.240 -4.160  1.00 15.61 ? 160 PHE A CE2 1 
ATOM   1264 C CZ  . PHE A 1 159 ? 21.603  -34.642 -4.148  1.00 18.42 ? 160 PHE A CZ  1 
ATOM   1265 N N   . GLY A 1 160 ? 22.969  -30.806 -8.187  1.00 17.65 ? 161 GLY A N   1 
ATOM   1266 C CA  . GLY A 1 160 ? 21.666  -30.261 -8.535  1.00 17.83 ? 161 GLY A CA  1 
ATOM   1267 C C   . GLY A 1 160 ? 21.321  -30.436 -10.005 1.00 19.20 ? 161 GLY A C   1 
ATOM   1268 O O   . GLY A 1 160 ? 20.165  -30.697 -10.354 1.00 18.65 ? 161 GLY A O   1 
ATOM   1269 N N   . LYS A 1 161 ? 22.308  -30.277 -10.889 1.00 19.19 ? 162 LYS A N   1 
ATOM   1270 C CA  . LYS A 1 161 ? 22.072  -30.531 -12.310 1.00 20.06 ? 162 LYS A CA  1 
ATOM   1271 C C   . LYS A 1 161 ? 21.620  -31.975 -12.547 1.00 20.01 ? 162 LYS A C   1 
ATOM   1272 O O   . LYS A 1 161 ? 20.678  -32.223 -13.312 1.00 18.42 ? 162 LYS A O   1 
ATOM   1273 C CB  . LYS A 1 161 ? 23.347  -30.210 -13.096 1.00 22.84 ? 162 LYS A CB  1 
ATOM   1274 C CG  . LYS A 1 161 ? 23.381  -30.746 -14.525 1.00 28.32 ? 162 LYS A CG  1 
ATOM   1275 C CD  . LYS A 1 161 ? 22.442  -29.983 -15.415 1.00 27.22 ? 162 LYS A CD  1 
ATOM   1276 C CE  . LYS A 1 161 ? 22.652  -30.334 -16.899 1.00 26.32 ? 162 LYS A CE  1 
ATOM   1277 N NZ  . LYS A 1 161 ? 21.918  -29.377 -17.770 1.00 28.51 ? 162 LYS A NZ  1 
ATOM   1278 N N   . VAL A 1 162 ? 22.266  -32.934 -11.879 1.00 17.53 ? 163 VAL A N   1 
ATOM   1279 C CA  . VAL A 1 162 ? 21.889  -34.349 -12.012 1.00 19.06 ? 163 VAL A CA  1 
ATOM   1280 C C   . VAL A 1 162 ? 20.480  -34.591 -11.472 1.00 19.08 ? 163 VAL A C   1 
ATOM   1281 O O   . VAL A 1 162 ? 19.684  -35.309 -12.091 1.00 18.76 ? 163 VAL A O   1 
ATOM   1282 C CB  . VAL A 1 162 ? 22.938  -35.238 -11.317 1.00 18.13 ? 163 VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 162 ? 22.455  -36.697 -11.163 1.00 18.78 ? 163 VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 162 ? 24.257  -35.183 -12.112 1.00 20.41 ? 163 VAL A CG2 1 
ATOM   1285 N N   . VAL A 1 163 ? 20.140  -33.985 -10.326 1.00 17.58 ? 164 VAL A N   1 
ATOM   1286 C CA  . VAL A 1 163 ? 18.785  -34.137 -9.781  1.00 16.92 ? 164 VAL A CA  1 
ATOM   1287 C C   . VAL A 1 163 ? 17.748  -33.672 -10.796 1.00 18.56 ? 164 VAL A C   1 
ATOM   1288 O O   . VAL A 1 163 ? 16.720  -34.330 -11.013 1.00 20.10 ? 164 VAL A O   1 
ATOM   1289 C CB  . VAL A 1 163 ? 18.646  -33.375 -8.446  1.00 19.80 ? 164 VAL A CB  1 
ATOM   1290 C CG1 . VAL A 1 163 ? 17.168  -33.267 -8.025  1.00 19.86 ? 164 VAL A CG1 1 
ATOM   1291 C CG2 . VAL A 1 163 ? 19.493  -34.044 -7.324  1.00 16.40 ? 164 VAL A CG2 1 
ATOM   1292 N N   . ALA A 1 164 ? 17.997  -32.529 -11.433 1.00 18.28 ? 165 ALA A N   1 
ATOM   1293 C CA  . ALA A 1 164 ? 17.062  -32.010 -12.421 1.00 19.31 ? 165 ALA A CA  1 
ATOM   1294 C C   . ALA A 1 164 ? 16.959  -32.941 -13.621 1.00 21.25 ? 165 ALA A C   1 
ATOM   1295 O O   . ALA A 1 164 ? 15.858  -33.211 -14.114 1.00 20.07 ? 165 ALA A O   1 
ATOM   1296 C CB  . ALA A 1 164 ? 17.487  -30.610 -12.856 1.00 20.35 ? 165 ALA A CB  1 
ATOM   1297 N N   . LEU A 1 165 ? 18.100  -33.420 -14.130 1.00 20.98 ? 166 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 165 ? 18.068  -34.370 -15.242 1.00 21.50 ? 166 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 165 ? 17.255  -35.609 -14.884 1.00 22.38 ? 166 LEU A C   1 
ATOM   1300 O O   . LEU A 1 165 ? 16.514  -36.138 -15.719 1.00 20.78 ? 166 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 165 ? 19.494  -34.773 -15.639 1.00 19.70 ? 166 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 165 ? 20.314  -33.736 -16.413 1.00 23.45 ? 166 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 165 ? 21.777  -34.151 -16.515 1.00 21.10 ? 166 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 165 ? 19.738  -33.505 -17.805 1.00 24.87 ? 166 LEU A CD2 1 
ATOM   1305 N N   . SER A 1 166 ? 17.368  -36.075 -13.642 1.00 20.03 ? 167 SER A N   1 
ATOM   1306 C CA  . SER A 1 166 ? 16.649  -37.284 -13.251 1.00 22.17 ? 167 SER A CA  1 
ATOM   1307 C C   . SER A 1 166 ? 15.145  -37.064 -13.193 1.00 21.57 ? 167 SER A C   1 
ATOM   1308 O O   . SER A 1 166 ? 14.385  -38.033 -13.281 1.00 22.72 ? 167 SER A O   1 
ATOM   1309 C CB  . SER A 1 166 ? 17.145  -37.774 -11.892 1.00 19.22 ? 167 SER A CB  1 
ATOM   1310 O OG  . SER A 1 166 ? 16.575  -37.009 -10.839 1.00 20.85 ? 167 SER A OG  1 
ATOM   1311 N N   . MET A 1 167 ? 14.701  -35.818 -13.041 1.00 19.27 ? 168 MET A N   1 
ATOM   1312 C CA  . MET A 1 167 ? 13.282  -35.485 -13.017 1.00 21.95 ? 168 MET A CA  1 
ATOM   1313 C C   . MET A 1 167 ? 12.784  -34.887 -14.332 1.00 25.58 ? 168 MET A C   1 
ATOM   1314 O O   . MET A 1 167 ? 11.629  -34.455 -14.393 1.00 24.35 ? 168 MET A O   1 
ATOM   1315 C CB  . MET A 1 167 ? 13.000  -34.522 -11.850 1.00 23.90 ? 168 MET A CB  1 
ATOM   1316 C CG  . MET A 1 167 ? 13.301  -35.140 -10.467 1.00 24.77 ? 168 MET A CG  1 
ATOM   1317 S SD  . MET A 1 167 ? 13.353  -33.946 -9.088  1.00 33.53 ? 168 MET A SD  1 
ATOM   1318 C CE  . MET A 1 167 ? 11.618  -33.492 -8.946  1.00 30.24 ? 168 MET A CE  1 
ATOM   1319 N N   . ASN A 1 168 ? 13.650  -34.809 -15.359 1.00 24.50 ? 169 ASN A N   1 
ATOM   1320 C CA  A ASN A 1 168 ? 13.276  -34.379 -16.712 0.43 25.47 ? 169 ASN A CA  1 
ATOM   1321 C CA  B ASN A 1 168 ? 13.276  -34.383 -16.713 0.57 25.00 ? 169 ASN A CA  1 
ATOM   1322 C C   . ASN A 1 168 ? 12.727  -32.952 -16.743 1.00 27.00 ? 169 ASN A C   1 
ATOM   1323 O O   . ASN A 1 168 ? 11.830  -32.628 -17.528 1.00 27.61 ? 169 ASN A O   1 
ATOM   1324 C CB  A ASN A 1 168 ? 12.280  -35.354 -17.342 0.43 28.56 ? 169 ASN A CB  1 
ATOM   1325 C CB  B ASN A 1 168 ? 12.277  -35.366 -17.335 0.57 27.95 ? 169 ASN A CB  1 
ATOM   1326 C CG  A ASN A 1 168 ? 12.820  -36.762 -17.409 0.43 27.06 ? 169 ASN A CG  1 
ATOM   1327 C CG  B ASN A 1 168 ? 12.107  -35.170 -18.829 0.57 28.07 ? 169 ASN A CG  1 
ATOM   1328 O OD1 A ASN A 1 168 ? 14.002  -36.968 -17.673 0.43 28.26 ? 169 ASN A OD1 1 
ATOM   1329 O OD1 B ASN A 1 168 ? 13.037  -34.768 -19.530 0.57 31.39 ? 169 ASN A OD1 1 
ATOM   1330 N ND2 A ASN A 1 168 ? 11.958  -37.744 -17.160 0.43 29.20 ? 169 ASN A ND2 1 
ATOM   1331 N ND2 B ASN A 1 168 ? 10.909  -35.458 -19.325 0.57 32.08 ? 169 ASN A ND2 1 
ATOM   1332 N N   . LYS A 1 169 ? 13.271  -32.085 -15.893 1.00 23.09 ? 170 LYS A N   1 
ATOM   1333 C CA  . LYS A 1 169 ? 12.926  -30.663 -15.845 1.00 24.64 ? 170 LYS A CA  1 
ATOM   1334 C C   . LYS A 1 169 ? 14.189  -29.863 -15.581 1.00 25.01 ? 170 LYS A C   1 
ATOM   1335 O O   . LYS A 1 169 ? 15.091  -30.349 -14.886 1.00 22.65 ? 170 LYS A O   1 
ATOM   1336 C CB  . LYS A 1 169 ? 11.926  -30.319 -14.724 1.00 27.78 ? 170 LYS A CB  1 
ATOM   1337 C CG  . LYS A 1 169 ? 10.639  -31.096 -14.659 1.00 33.91 ? 170 LYS A CG  1 
ATOM   1338 C CD  . LYS A 1 169 ? 9.914   -30.760 -13.343 1.00 34.86 ? 170 LYS A CD  1 
ATOM   1339 C CE  . LYS A 1 169 ? 8.819   -31.782 -13.025 1.00 41.24 ? 170 LYS A CE  1 
ATOM   1340 N NZ  . LYS A 1 169 ? 9.366   -33.086 -12.504 1.00 37.82 ? 170 LYS A NZ  1 
ATOM   1341 N N   . PRO A 1 170 ? 14.268  -28.617 -16.065 1.00 23.36 ? 171 PRO A N   1 
ATOM   1342 C CA  . PRO A 1 170 ? 15.362  -27.743 -15.617 1.00 25.30 ? 171 PRO A CA  1 
ATOM   1343 C C   . PRO A 1 170 ? 15.290  -27.509 -14.111 1.00 22.48 ? 171 PRO A C   1 
ATOM   1344 O O   . PRO A 1 170 ? 14.223  -27.554 -13.501 1.00 19.51 ? 171 PRO A O   1 
ATOM   1345 C CB  . PRO A 1 170 ? 15.152  -26.442 -16.408 1.00 23.28 ? 171 PRO A CB  1 
ATOM   1346 C CG  . PRO A 1 170 ? 13.829  -26.580 -17.140 1.00 26.98 ? 171 PRO A CG  1 
ATOM   1347 C CD  . PRO A 1 170 ? 13.487  -28.039 -17.179 1.00 27.83 ? 171 PRO A CD  1 
ATOM   1348 N N   . PHE A 1 171 ? 16.452  -27.257 -13.512 1.00 19.95 ? 172 PHE A N   1 
ATOM   1349 C CA  . PHE A 1 171 ? 16.514  -27.126 -12.057 1.00 20.62 ? 172 PHE A CA  1 
ATOM   1350 C C   . PHE A 1 171 ? 15.555  -26.052 -11.532 1.00 21.72 ? 172 PHE A C   1 
ATOM   1351 O O   . PHE A 1 171 ? 14.919  -26.246 -10.492 1.00 20.25 ? 172 PHE A O   1 
ATOM   1352 C CB  . PHE A 1 171 ? 17.958  -26.841 -11.624 1.00 19.49 ? 172 PHE A CB  1 
ATOM   1353 C CG  . PHE A 1 171 ? 18.126  -26.695 -10.125 1.00 19.81 ? 172 PHE A CG  1 
ATOM   1354 C CD1 . PHE A 1 171 ? 18.251  -27.812 -9.319  1.00 20.05 ? 172 PHE A CD1 1 
ATOM   1355 C CD2 . PHE A 1 171 ? 18.167  -25.436 -9.529  1.00 20.63 ? 172 PHE A CD2 1 
ATOM   1356 C CE1 . PHE A 1 171 ? 18.402  -27.683 -7.942  1.00 19.83 ? 172 PHE A CE1 1 
ATOM   1357 C CE2 . PHE A 1 171 ? 18.325  -25.306 -8.158  1.00 20.98 ? 172 PHE A CE2 1 
ATOM   1358 C CZ  . PHE A 1 171 ? 18.444  -26.432 -7.366  1.00 17.54 ? 172 PHE A CZ  1 
ATOM   1359 N N   . ASP A 1 172 ? 15.440  -24.907 -12.225 1.00 20.07 ? 173 ASP A N   1 
ATOM   1360 C CA  . ASP A 1 172 ? 14.539  -23.858 -11.740 1.00 21.62 ? 173 ASP A CA  1 
ATOM   1361 C C   . ASP A 1 172 ? 13.109  -24.369 -11.645 1.00 24.64 ? 173 ASP A C   1 
ATOM   1362 O O   . ASP A 1 172 ? 12.363  -24.008 -10.724 1.00 22.02 ? 173 ASP A O   1 
ATOM   1363 C CB  . ASP A 1 172 ? 14.610  -22.618 -12.654 1.00 26.41 ? 173 ASP A CB  1 
ATOM   1364 C CG  . ASP A 1 172 ? 14.036  -22.880 -14.061 1.00 31.38 ? 173 ASP A CG  1 
ATOM   1365 O OD1 . ASP A 1 172 ? 14.636  -23.662 -14.821 1.00 34.10 ? 173 ASP A OD1 1 
ATOM   1366 O OD2 . ASP A 1 172 ? 12.971  -22.325 -14.405 1.00 37.25 ? 173 ASP A OD2 1 
ATOM   1367 N N   . GLN A 1 173 ? 12.711  -25.230 -12.582 1.00 24.21 ? 174 GLN A N   1 
ATOM   1368 C CA  A GLN A 1 173 ? 11.374  -25.807 -12.548 0.58 24.65 ? 174 GLN A CA  1 
ATOM   1369 C CA  B GLN A 1 173 ? 11.370  -25.796 -12.539 0.42 24.31 ? 174 GLN A CA  1 
ATOM   1370 C C   . GLN A 1 173 ? 11.238  -26.872 -11.467 1.00 22.74 ? 174 GLN A C   1 
ATOM   1371 O O   . GLN A 1 173 ? 10.159  -27.037 -10.901 1.00 23.68 ? 174 GLN A O   1 
ATOM   1372 C CB  A GLN A 1 173 ? 11.043  -26.382 -13.918 0.58 25.38 ? 174 GLN A CB  1 
ATOM   1373 C CB  B GLN A 1 173 ? 10.992  -26.355 -13.911 0.42 25.47 ? 174 GLN A CB  1 
ATOM   1374 C CG  A GLN A 1 173 ? 10.856  -25.309 -14.961 0.58 27.87 ? 174 GLN A CG  1 
ATOM   1375 C CG  B GLN A 1 173 ? 10.902  -25.294 -15.006 0.42 27.84 ? 174 GLN A CG  1 
ATOM   1376 C CD  A GLN A 1 173 ? 9.580   -24.542 -14.741 0.58 27.42 ? 174 GLN A CD  1 
ATOM   1377 C CD  B GLN A 1 173 ? 10.306  -25.824 -16.301 0.42 27.83 ? 174 GLN A CD  1 
ATOM   1378 O OE1 A GLN A 1 173 ? 8.526   -24.941 -15.232 0.58 32.49 ? 174 GLN A OE1 1 
ATOM   1379 O OE1 B GLN A 1 173 ? 9.784   -26.938 -16.349 0.42 26.75 ? 174 GLN A OE1 1 
ATOM   1380 N NE2 A GLN A 1 173 ? 9.658   -23.439 -13.998 0.58 30.82 ? 174 GLN A NE2 1 
ATOM   1381 N NE2 B GLN A 1 173 ? 10.371  -25.018 -17.358 0.42 31.49 ? 174 GLN A NE2 1 
ATOM   1382 N N   . VAL A 1 174 ? 12.306  -27.610 -11.174 1.00 18.68 ? 175 VAL A N   1 
ATOM   1383 C CA  . VAL A 1 174 ? 12.241  -28.556 -10.060 1.00 21.80 ? 175 VAL A CA  1 
ATOM   1384 C C   . VAL A 1 174 ? 11.822  -27.825 -8.788  1.00 21.78 ? 175 VAL A C   1 
ATOM   1385 O O   . VAL A 1 174 ? 10.916  -28.263 -8.066  1.00 19.51 ? 175 VAL A O   1 
ATOM   1386 C CB  . VAL A 1 174 ? 13.585  -29.287 -9.878  1.00 21.45 ? 175 VAL A CB  1 
ATOM   1387 C CG1 . VAL A 1 174 ? 13.554  -30.112 -8.580  1.00 20.18 ? 175 VAL A CG1 1 
ATOM   1388 C CG2 . VAL A 1 174 ? 13.869  -30.192 -11.089 1.00 24.80 ? 175 VAL A CG2 1 
ATOM   1389 N N   . LEU A 1 175 ? 12.440  -26.668 -8.525  1.00 20.79 ? 176 LEU A N   1 
ATOM   1390 C CA  . LEU A 1 175 ? 12.084  -25.915 -7.325  1.00 19.36 ? 176 LEU A CA  1 
ATOM   1391 C C   . LEU A 1 175 ? 10.724  -25.239 -7.477  1.00 22.67 ? 176 LEU A C   1 
ATOM   1392 O O   . LEU A 1 175 ? 9.862   -25.360 -6.601  1.00 19.72 ? 176 LEU A O   1 
ATOM   1393 C CB  . LEU A 1 175 ? 13.170  -24.885 -6.990  1.00 19.32 ? 176 LEU A CB  1 
ATOM   1394 C CG  . LEU A 1 175 ? 14.533  -25.485 -6.583  1.00 18.77 ? 176 LEU A CG  1 
ATOM   1395 C CD1 . LEU A 1 175 ? 15.412  -24.397 -6.007  1.00 18.43 ? 176 LEU A CD1 1 
ATOM   1396 C CD2 . LEU A 1 175 ? 14.365  -26.607 -5.563  1.00 19.87 ? 176 LEU A CD2 1 
ATOM   1397 N N   . GLU A 1 176 ? 10.508  -24.507 -8.580  1.00 21.56 ? 177 GLU A N   1 
ATOM   1398 C CA  . GLU A 1 176 ? 9.319   -23.659 -8.646  1.00 23.62 ? 177 GLU A CA  1 
ATOM   1399 C C   . GLU A 1 176 ? 8.044   -24.458 -8.878  1.00 22.61 ? 177 GLU A C   1 
ATOM   1400 O O   . GLU A 1 176 ? 6.970   -24.037 -8.431  1.00 23.33 ? 177 GLU A O   1 
ATOM   1401 C CB  . GLU A 1 176 ? 9.495   -22.570 -9.722  1.00 25.98 ? 177 GLU A CB  1 
ATOM   1402 C CG  . GLU A 1 176 ? 10.602  -21.597 -9.317  1.00 22.44 ? 177 GLU A CG  1 
ATOM   1403 C CD  . GLU A 1 176 ? 10.753  -20.374 -10.223 1.00 29.64 ? 177 GLU A CD  1 
ATOM   1404 O OE1 . GLU A 1 176 ? 10.119  -20.306 -11.301 1.00 27.13 ? 177 GLU A OE1 1 
ATOM   1405 O OE2 . GLU A 1 176 ? 11.519  -19.472 -9.833  1.00 25.38 ? 177 GLU A OE2 1 
ATOM   1406 N N   . LYS A 1 177 ? 8.129   -25.616 -9.536  1.00 24.28 ? 178 LYS A N   1 
ATOM   1407 C CA  . LYS A 1 177 ? 6.925   -26.375 -9.851  1.00 25.12 ? 178 LYS A CA  1 
ATOM   1408 C C   . LYS A 1 177 ? 6.714   -27.595 -8.957  1.00 24.44 ? 178 LYS A C   1 
ATOM   1409 O O   . LYS A 1 177 ? 5.575   -28.048 -8.826  1.00 23.69 ? 178 LYS A O   1 
ATOM   1410 C CB  . LYS A 1 177 ? 6.948   -26.826 -11.318 1.00 27.84 ? 178 LYS A CB  1 
ATOM   1411 C CG  . LYS A 1 177 ? 6.855   -25.673 -12.321 1.00 28.38 ? 178 LYS A CG  1 
ATOM   1412 C CD  . LYS A 1 177 ? 5.733   -25.888 -13.319 1.00 37.82 ? 178 LYS A CD  1 
ATOM   1413 C CE  . LYS A 1 177 ? 5.534   -24.661 -14.214 1.00 39.05 ? 178 LYS A CE  1 
ATOM   1414 N NZ  . LYS A 1 177 ? 5.306   -23.420 -13.420 1.00 45.84 ? 178 LYS A NZ  1 
ATOM   1415 N N   . THR A 1 178 ? 7.761   -28.126 -8.330  1.00 21.58 ? 179 THR A N   1 
ATOM   1416 C CA  . THR A 1 178 ? 7.631   -29.317 -7.496  1.00 22.44 ? 179 THR A CA  1 
ATOM   1417 C C   . THR A 1 178 ? 7.949   -29.047 -6.029  1.00 22.39 ? 179 THR A C   1 
ATOM   1418 O O   . THR A 1 178 ? 7.093   -29.288 -5.175  1.00 20.80 ? 179 THR A O   1 
ATOM   1419 C CB  . THR A 1 178 ? 8.523   -30.445 -8.037  1.00 22.50 ? 179 THR A CB  1 
ATOM   1420 O OG1 . THR A 1 178 ? 8.144   -30.742 -9.389  1.00 26.65 ? 179 THR A OG1 1 
ATOM   1421 C CG2 . THR A 1 178 ? 8.365   -31.693 -7.183  1.00 23.21 ? 179 THR A CG2 1 
ATOM   1422 N N   . ILE A 1 179 ? 9.143   -28.548 -5.704  1.00 18.89 ? 180 ILE A N   1 
ATOM   1423 C CA  . ILE A 1 179 ? 9.580   -28.515 -4.308  1.00 17.31 ? 180 ILE A CA  1 
ATOM   1424 C C   . ILE A 1 179 ? 8.920   -27.366 -3.542  1.00 19.77 ? 180 ILE A C   1 
ATOM   1425 O O   . ILE A 1 179 ? 8.388   -27.562 -2.440  1.00 19.57 ? 180 ILE A O   1 
ATOM   1426 C CB  . ILE A 1 179 ? 11.118  -28.438 -4.244  1.00 16.34 ? 180 ILE A CB  1 
ATOM   1427 C CG1 . ILE A 1 179 ? 11.745  -29.668 -4.916  1.00 16.40 ? 180 ILE A CG1 1 
ATOM   1428 C CG2 . ILE A 1 179 ? 11.586  -28.337 -2.807  1.00 16.80 ? 180 ILE A CG2 1 
ATOM   1429 C CD1 . ILE A 1 179 ? 11.309  -30.968 -4.265  1.00 17.63 ? 180 ILE A CD1 1 
ATOM   1430 N N   . PHE A 1 180 ? 8.920   -26.153 -4.108  1.00 17.98 ? 181 PHE A N   1 
ATOM   1431 C CA  . PHE A 1 180 ? 8.300   -25.025 -3.409  1.00 20.06 ? 181 PHE A CA  1 
ATOM   1432 C C   . PHE A 1 180 ? 6.808   -25.250 -3.161  1.00 20.08 ? 181 PHE A C   1 
ATOM   1433 O O   . PHE A 1 180 ? 6.356   -25.045 -2.022  1.00 19.40 ? 181 PHE A O   1 
ATOM   1434 C CB  . PHE A 1 180 ? 8.520   -23.713 -4.186  1.00 21.06 ? 181 PHE A CB  1 
ATOM   1435 C CG  . PHE A 1 180 ? 9.959   -23.217 -4.216  1.00 22.30 ? 181 PHE A CG  1 
ATOM   1436 C CD1 . PHE A 1 180 ? 10.888  -23.611 -3.269  1.00 19.24 ? 181 PHE A CD1 1 
ATOM   1437 C CD2 . PHE A 1 180 ? 10.356  -22.296 -5.199  1.00 24.12 ? 181 PHE A CD2 1 
ATOM   1438 C CE1 . PHE A 1 180 ? 12.223  -23.117 -3.308  1.00 20.76 ? 181 PHE A CE1 1 
ATOM   1439 C CE2 . PHE A 1 180 ? 11.668  -21.804 -5.254  1.00 23.24 ? 181 PHE A CE2 1 
ATOM   1440 C CZ  . PHE A 1 180 ? 12.599  -22.208 -4.311  1.00 21.27 ? 181 PHE A CZ  1 
ATOM   1441 N N   . PRO A 1 181 ? 6.002   -25.677 -4.140  1.00 19.97 ? 182 PRO A N   1 
ATOM   1442 C CA  . PRO A 1 181 ? 4.590   -25.949 -3.835  1.00 22.62 ? 182 PRO A CA  1 
ATOM   1443 C C   . PRO A 1 181 ? 4.400   -27.064 -2.820  1.00 24.02 ? 182 PRO A C   1 
ATOM   1444 O O   . PRO A 1 181 ? 3.491   -26.971 -1.985  1.00 23.44 ? 182 PRO A O   1 
ATOM   1445 C CB  . PRO A 1 181 ? 4.002   -26.328 -5.200  1.00 25.43 ? 182 PRO A CB  1 
ATOM   1446 C CG  . PRO A 1 181 ? 4.924   -25.730 -6.192  1.00 25.56 ? 182 PRO A CG  1 
ATOM   1447 C CD  . PRO A 1 181 ? 6.281   -25.809 -5.582  1.00 21.97 ? 182 PRO A CD  1 
ATOM   1448 N N   . ALA A 1 182 ? 5.232   -28.112 -2.863  1.00 22.20 ? 183 ALA A N   1 
ATOM   1449 C CA  . ALA A 1 182 ? 5.108   -29.198 -1.887  1.00 21.96 ? 183 ALA A CA  1 
ATOM   1450 C C   . ALA A 1 182 ? 5.366   -28.715 -0.462  1.00 23.32 ? 183 ALA A C   1 
ATOM   1451 O O   . ALA A 1 182 ? 4.857   -29.314 0.501   1.00 21.16 ? 183 ALA A O   1 
ATOM   1452 C CB  . ALA A 1 182 ? 6.073   -30.336 -2.223  1.00 20.65 ? 183 ALA A CB  1 
ATOM   1453 N N   . LEU A 1 183 ? 6.151   -27.650 -0.304  1.00 23.87 ? 184 LEU A N   1 
ATOM   1454 C CA  . LEU A 1 183 ? 6.453   -27.083 1.007   1.00 23.81 ? 184 LEU A CA  1 
ATOM   1455 C C   . LEU A 1 183 ? 5.530   -25.937 1.378   1.00 25.29 ? 184 LEU A C   1 
ATOM   1456 O O   . LEU A 1 183 ? 5.700   -25.349 2.449   1.00 26.76 ? 184 LEU A O   1 
ATOM   1457 C CB  . LEU A 1 183 ? 7.910   -26.598 1.070   1.00 19.00 ? 184 LEU A CB  1 
ATOM   1458 C CG  . LEU A 1 183 ? 9.028   -27.635 0.953   1.00 21.68 ? 184 LEU A CG  1 
ATOM   1459 C CD1 . LEU A 1 183 ? 10.349  -26.941 0.606   1.00 21.61 ? 184 LEU A CD1 1 
ATOM   1460 C CD2 . LEU A 1 183 ? 9.178   -28.476 2.240   1.00 21.73 ? 184 LEU A CD2 1 
ATOM   1461 N N   . GLY A 1 184 ? 4.574   -25.600 0.519   1.00 25.74 ? 185 GLY A N   1 
ATOM   1462 C CA  . GLY A 1 184 ? 3.652   -24.527 0.807   1.00 28.06 ? 185 GLY A CA  1 
ATOM   1463 C C   . GLY A 1 184 ? 4.245   -23.144 0.691   1.00 25.80 ? 185 GLY A C   1 
ATOM   1464 O O   . GLY A 1 184 ? 3.728   -22.213 1.301   1.00 30.41 ? 185 GLY A O   1 
ATOM   1465 N N   . LEU A 1 185 ? 5.329   -22.978 -0.062  1.00 24.97 ? 186 LEU A N   1 
ATOM   1466 C CA  . LEU A 1 185 ? 5.955   -21.669 -0.207  1.00 23.49 ? 186 LEU A CA  1 
ATOM   1467 C C   . LEU A 1 185 ? 5.377   -20.973 -1.428  1.00 31.09 ? 186 LEU A C   1 
ATOM   1468 O O   . LEU A 1 185 ? 5.386   -21.535 -2.527  1.00 33.58 ? 186 LEU A O   1 
ATOM   1469 C CB  . LEU A 1 185 ? 7.472   -21.807 -0.332  1.00 24.24 ? 186 LEU A CB  1 
ATOM   1470 C CG  . LEU A 1 185 ? 8.063   -22.712 0.750   1.00 22.90 ? 186 LEU A CG  1 
ATOM   1471 C CD1 . LEU A 1 185 ? 9.572   -22.873 0.603   1.00 24.06 ? 186 LEU A CD1 1 
ATOM   1472 C CD2 . LEU A 1 185 ? 7.713   -22.236 2.162   1.00 23.07 ? 186 LEU A CD2 1 
ATOM   1473 N N   . LYS A 1 186 ? 4.888   -19.744 -1.244  1.00 25.22 ? 187 LYS A N   1 
ATOM   1474 C CA  . LYS A 1 186 ? 4.218   -19.050 -2.326  1.00 28.83 ? 187 LYS A CA  1 
ATOM   1475 C C   . LYS A 1 186 ? 4.978   -17.836 -2.840  1.00 28.65 ? 187 LYS A C   1 
ATOM   1476 O O   . LYS A 1 186 ? 4.556   -17.249 -3.837  1.00 27.77 ? 187 LYS A O   1 
ATOM   1477 C CB  . LYS A 1 186 ? 2.803   -18.646 -1.885  1.00 35.35 ? 187 LYS A CB  1 
ATOM   1478 C CG  . LYS A 1 186 ? 1.956   -19.838 -1.452  1.00 35.27 ? 187 LYS A CG  1 
ATOM   1479 C CD  . LYS A 1 186 ? 2.108   -20.994 -2.449  1.00 41.11 ? 187 LYS A CD  1 
ATOM   1480 C CE  . LYS A 1 186 ? 1.547   -22.320 -1.918  1.00 37.44 ? 187 LYS A CE  1 
ATOM   1481 N NZ  . LYS A 1 186 ? 2.038   -23.513 -2.697  1.00 40.94 ? 187 LYS A NZ  1 
ATOM   1482 N N   . HIS A 1 187 ? 6.096   -17.456 -2.215  1.00 23.71 ? 188 HIS A N   1 
ATOM   1483 C CA  . HIS A 1 187 ? 6.874   -16.307 -2.672  1.00 27.76 ? 188 HIS A CA  1 
ATOM   1484 C C   . HIS A 1 187 ? 8.370   -16.613 -2.590  1.00 26.45 ? 188 HIS A C   1 
ATOM   1485 O O   . HIS A 1 187 ? 9.184   -15.774 -2.186  1.00 25.98 ? 188 HIS A O   1 
ATOM   1486 C CB  . HIS A 1 187 ? 6.494   -15.048 -1.894  1.00 27.17 ? 188 HIS A CB  1 
ATOM   1487 C CG  . HIS A 1 187 ? 5.085   -14.597 -2.155  1.00 27.63 ? 188 HIS A CG  1 
ATOM   1488 N ND1 . HIS A 1 187 ? 4.077   -14.722 -1.225  1.00 29.29 ? 188 HIS A ND1 1 
ATOM   1489 C CD2 . HIS A 1 187 ? 4.511   -14.067 -3.261  1.00 28.37 ? 188 HIS A CD2 1 
ATOM   1490 C CE1 . HIS A 1 187 ? 2.945   -14.271 -1.739  1.00 29.09 ? 188 HIS A CE1 1 
ATOM   1491 N NE2 . HIS A 1 187 ? 3.180   -13.868 -2.974  1.00 29.12 ? 188 HIS A NE2 1 
ATOM   1492 N N   . SER A 1 188 ? 8.740   -17.819 -3.002  1.00 22.39 ? 189 SER A N   1 
ATOM   1493 C CA  . SER A 1 188 ? 10.123  -18.261 -3.102  1.00 22.75 ? 189 SER A CA  1 
ATOM   1494 C C   . SER A 1 188 ? 10.411  -18.580 -4.563  1.00 23.14 ? 189 SER A C   1 
ATOM   1495 O O   . SER A 1 188 ? 9.551   -19.125 -5.263  1.00 22.24 ? 189 SER A O   1 
ATOM   1496 C CB  . SER A 1 188 ? 10.354  -19.484 -2.210  1.00 23.18 ? 189 SER A CB  1 
ATOM   1497 O OG  . SER A 1 188 ? 9.886   -19.188 -0.903  1.00 21.93 ? 189 SER A OG  1 
ATOM   1498 N N   . TYR A 1 189 ? 11.605  -18.215 -5.032  1.00 22.66 ? 190 TYR A N   1 
ATOM   1499 C CA  . TYR A 1 189 ? 11.865  -18.158 -6.465  1.00 22.37 ? 190 TYR A CA  1 
ATOM   1500 C C   . TYR A 1 189 ? 13.318  -18.477 -6.766  1.00 24.18 ? 190 TYR A C   1 
ATOM   1501 O O   . TYR A 1 189 ? 14.212  -18.180 -5.971  1.00 23.65 ? 190 TYR A O   1 
ATOM   1502 C CB  . TYR A 1 189 ? 11.567  -16.763 -7.057  1.00 25.02 ? 190 TYR A CB  1 
ATOM   1503 C CG  . TYR A 1 189 ? 10.181  -16.261 -6.776  1.00 26.49 ? 190 TYR A CG  1 
ATOM   1504 C CD1 . TYR A 1 189 ? 9.103   -16.680 -7.548  1.00 26.27 ? 190 TYR A CD1 1 
ATOM   1505 C CD2 . TYR A 1 189 ? 9.944   -15.363 -5.739  1.00 25.79 ? 190 TYR A CD2 1 
ATOM   1506 C CE1 . TYR A 1 189 ? 7.822   -16.235 -7.283  1.00 29.44 ? 190 TYR A CE1 1 
ATOM   1507 C CE2 . TYR A 1 189 ? 8.670   -14.902 -5.476  1.00 28.68 ? 190 TYR A CE2 1 
ATOM   1508 C CZ  . TYR A 1 189 ? 7.614   -15.337 -6.251  1.00 29.07 ? 190 TYR A CZ  1 
ATOM   1509 O OH  . TYR A 1 189 ? 6.348   -14.881 -5.975  1.00 27.73 ? 190 TYR A OH  1 
ATOM   1510 N N   . VAL A 1 190 ? 13.540  -19.064 -7.942  1.00 23.32 ? 191 VAL A N   1 
ATOM   1511 C CA  . VAL A 1 190 ? 14.838  -18.955 -8.603  1.00 23.25 ? 191 VAL A CA  1 
ATOM   1512 C C   . VAL A 1 190 ? 14.875  -17.748 -9.536  1.00 27.18 ? 191 VAL A C   1 
ATOM   1513 O O   . VAL A 1 190 ? 15.883  -17.048 -9.608  1.00 25.70 ? 191 VAL A O   1 
ATOM   1514 C CB  . VAL A 1 190 ? 15.174  -20.249 -9.359  1.00 26.37 ? 191 VAL A CB  1 
ATOM   1515 C CG1 . VAL A 1 190 ? 16.497  -20.078 -10.116 1.00 26.36 ? 191 VAL A CG1 1 
ATOM   1516 C CG2 . VAL A 1 190 ? 15.266  -21.420 -8.371  1.00 24.90 ? 191 VAL A CG2 1 
ATOM   1517 N N   . ASN A 1 191 ? 13.795  -17.497 -10.270 1.00 24.57 ? 192 ASN A N   1 
ATOM   1518 C CA  . ASN A 1 191 ? 13.650  -16.297 -11.090 1.00 27.69 ? 192 ASN A CA  1 
ATOM   1519 C C   . ASN A 1 191 ? 12.466  -15.496 -10.559 1.00 28.62 ? 192 ASN A C   1 
ATOM   1520 O O   . ASN A 1 191 ? 11.325  -15.965 -10.603 1.00 29.50 ? 192 ASN A O   1 
ATOM   1521 C CB  . ASN A 1 191 ? 13.454  -16.660 -12.570 1.00 29.24 ? 192 ASN A CB  1 
ATOM   1522 C CG  . ASN A 1 191 ? 14.605  -17.480 -13.135 1.00 34.31 ? 192 ASN A CG  1 
ATOM   1523 O OD1 . ASN A 1 191 ? 14.464  -18.683 -13.405 1.00 35.94 ? 192 ASN A OD1 1 
ATOM   1524 N ND2 . ASN A 1 191 ? 15.758  -16.839 -13.309 1.00 31.17 ? 192 ASN A ND2 1 
ATOM   1525 N N   . VAL A 1 192 ? 12.733  -14.297 -10.051 1.00 28.54 ? 193 VAL A N   1 
ATOM   1526 C CA  . VAL A 1 192 ? 11.671  -13.439 -9.523  1.00 30.16 ? 193 VAL A CA  1 
ATOM   1527 C C   . VAL A 1 192 ? 10.813  -12.919 -10.672 1.00 30.34 ? 193 VAL A C   1 
ATOM   1528 O O   . VAL A 1 192 ? 11.345  -12.290 -11.594 1.00 30.74 ? 193 VAL A O   1 
ATOM   1529 C CB  . VAL A 1 192 ? 12.257  -12.276 -8.704  1.00 30.59 ? 193 VAL A CB  1 
ATOM   1530 C CG1 . VAL A 1 192 ? 11.148  -11.353 -8.228  1.00 31.25 ? 193 VAL A CG1 1 
ATOM   1531 C CG2 . VAL A 1 192 ? 13.061  -12.811 -7.517  1.00 27.85 ? 193 VAL A CG2 1 
ATOM   1532 N N   . PRO A 1 193 ? 9.497   -13.137 -10.655 1.00 29.41 ? 194 PRO A N   1 
ATOM   1533 C CA  . PRO A 1 193 ? 8.640   -12.640 -11.741 1.00 31.10 ? 194 PRO A CA  1 
ATOM   1534 C C   . PRO A 1 193 ? 8.524   -11.122 -11.719 1.00 35.60 ? 194 PRO A C   1 
ATOM   1535 O O   . PRO A 1 193 ? 8.709   -10.472 -10.687 1.00 33.18 ? 194 PRO A O   1 
ATOM   1536 C CB  . PRO A 1 193 ? 7.278   -13.285 -11.451 1.00 32.22 ? 194 PRO A CB  1 
ATOM   1537 C CG  . PRO A 1 193 ? 7.517   -14.299 -10.370 1.00 38.28 ? 194 PRO A CG  1 
ATOM   1538 C CD  . PRO A 1 193 ? 8.735   -13.874 -9.636  1.00 33.77 ? 194 PRO A CD  1 
ATOM   1539 N N   . LYS A 1 194 ? 8.160   -10.557 -12.879 1.00 35.16 ? 195 LYS A N   1 
ATOM   1540 C CA  . LYS A 1 194 ? 8.069   -9.102  -12.983 1.00 35.64 ? 195 LYS A CA  1 
ATOM   1541 C C   . LYS A 1 194 ? 7.028   -8.527  -12.027 1.00 36.22 ? 195 LYS A C   1 
ATOM   1542 O O   . LYS A 1 194 ? 7.208   -7.419  -11.506 1.00 38.32 ? 195 LYS A O   1 
ATOM   1543 C CB  . LYS A 1 194 ? 7.761   -8.685  -14.424 1.00 40.32 ? 195 LYS A CB  1 
ATOM   1544 C CG  . LYS A 1 194 ? 7.825   -7.165  -14.655 1.00 46.59 ? 195 LYS A CG  1 
ATOM   1545 C CD  . LYS A 1 194 ? 9.188   -6.602  -14.221 1.00 51.77 ? 195 LYS A CD  1 
ATOM   1546 C CE  . LYS A 1 194 ? 9.221   -5.071  -14.209 1.00 50.80 ? 195 LYS A CE  1 
ATOM   1547 N NZ  . LYS A 1 194 ? 9.202   -4.472  -15.581 1.00 57.29 ? 195 LYS A NZ  1 
ATOM   1548 N N   . THR A 1 195 ? 5.946   -9.259  -11.771 1.00 36.86 ? 196 THR A N   1 
ATOM   1549 C CA  . THR A 1 195 ? 4.944   -8.780  -10.827 1.00 40.05 ? 196 THR A CA  1 
ATOM   1550 C C   . THR A 1 195 ? 5.454   -8.740  -9.388  1.00 36.76 ? 196 THR A C   1 
ATOM   1551 O O   . THR A 1 195 ? 4.731   -8.254  -8.511  1.00 37.86 ? 196 THR A O   1 
ATOM   1552 C CB  . THR A 1 195 ? 3.677   -9.641  -10.908 1.00 37.78 ? 196 THR A CB  1 
ATOM   1553 O OG1 . THR A 1 195 ? 3.976   -10.983 -10.509 1.00 41.30 ? 196 THR A OG1 1 
ATOM   1554 C CG2 . THR A 1 195 ? 3.124   -9.646  -12.328 1.00 39.15 ? 196 THR A CG2 1 
ATOM   1555 N N   . GLN A 1 196 ? 6.675   -9.215  -9.127  1.00 35.99 ? 197 GLN A N   1 
ATOM   1556 C CA  . GLN A 1 196 ? 7.262   -9.197  -7.791  1.00 34.19 ? 197 GLN A CA  1 
ATOM   1557 C C   . GLN A 1 196 ? 8.533   -8.356  -7.702  1.00 35.10 ? 197 GLN A C   1 
ATOM   1558 O O   . GLN A 1 196 ? 9.158   -8.324  -6.636  1.00 30.57 ? 197 GLN A O   1 
ATOM   1559 C CB  . GLN A 1 196 ? 7.563   -10.628 -7.325  1.00 30.03 ? 197 GLN A CB  1 
ATOM   1560 C CG  . GLN A 1 196 ? 6.329   -11.434 -7.025  1.00 31.64 ? 197 GLN A CG  1 
ATOM   1561 C CD  . GLN A 1 196 ? 5.641   -10.998 -5.745  1.00 33.02 ? 197 GLN A CD  1 
ATOM   1562 O OE1 . GLN A 1 196 ? 6.283   -10.527 -4.796  1.00 31.98 ? 197 GLN A OE1 1 
ATOM   1563 N NE2 . GLN A 1 196 ? 4.328   -11.154 -5.708  1.00 34.06 ? 197 GLN A NE2 1 
ATOM   1564 N N   . MET A 1 197 ? 8.930   -7.671  -8.781  1.00 32.53 ? 198 MET A N   1 
ATOM   1565 C CA  . MET A 1 197 ? 10.184  -6.917  -8.766  1.00 36.09 ? 198 MET A CA  1 
ATOM   1566 C C   . MET A 1 197 ? 10.178  -5.811  -7.713  1.00 34.90 ? 198 MET A C   1 
ATOM   1567 O O   . MET A 1 197 ? 11.222  -5.512  -7.118  1.00 33.02 ? 198 MET A O   1 
ATOM   1568 C CB  . MET A 1 197 ? 10.463  -6.318  -10.148 1.00 38.72 ? 198 MET A CB  1 
ATOM   1569 C CG  . MET A 1 197 ? 11.057  -7.307  -11.141 1.00 44.37 ? 198 MET A CG  1 
ATOM   1570 S SD  . MET A 1 197 ? 12.555  -8.124  -10.534 1.00 58.02 ? 198 MET A SD  1 
ATOM   1571 C CE  . MET A 1 197 ? 12.724  -9.429  -11.746 1.00 44.21 ? 198 MET A CE  1 
ATOM   1572 N N   . GLN A 1 198 ? 9.029   -5.193  -7.468  1.00 34.77 ? 199 GLN A N   1 
ATOM   1573 C CA  . GLN A 1 198 ? 8.971   -4.148  -6.455  1.00 32.13 ? 199 GLN A CA  1 
ATOM   1574 C C   . GLN A 1 198 ? 9.136   -4.689  -5.036  1.00 33.42 ? 199 GLN A C   1 
ATOM   1575 O O   . GLN A 1 198 ? 9.325   -3.888  -4.116  1.00 33.78 ? 199 GLN A O   1 
ATOM   1576 C CB  . GLN A 1 198 ? 7.656   -3.376  -6.581  1.00 38.73 ? 199 GLN A CB  1 
ATOM   1577 C CG  . GLN A 1 198 ? 6.407   -4.189  -6.246  1.00 43.31 ? 199 GLN A CG  1 
ATOM   1578 C CD  . GLN A 1 198 ? 6.050   -5.228  -7.307  1.00 48.91 ? 199 GLN A CD  1 
ATOM   1579 O OE1 . GLN A 1 198 ? 6.740   -5.372  -8.329  1.00 45.36 ? 199 GLN A OE1 1 
ATOM   1580 N NE2 . GLN A 1 198 ? 4.958   -5.950  -7.072  1.00 51.10 ? 199 GLN A NE2 1 
ATOM   1581 N N   . ASN A 1 199 ? 9.079   -6.011  -4.837  1.00 31.66 ? 200 ASN A N   1 
ATOM   1582 C CA  . ASN A 1 199 ? 9.305   -6.637  -3.535  1.00 31.33 ? 200 ASN A CA  1 
ATOM   1583 C C   . ASN A 1 199 ? 10.707  -7.211  -3.380  1.00 29.86 ? 200 ASN A C   1 
ATOM   1584 O O   . ASN A 1 199 ? 11.052  -7.700  -2.293  1.00 30.22 ? 200 ASN A O   1 
ATOM   1585 C CB  . ASN A 1 199 ? 8.284   -7.753  -3.293  1.00 27.12 ? 200 ASN A CB  1 
ATOM   1586 C CG  . ASN A 1 199 ? 6.886   -7.224  -3.139  1.00 35.16 ? 200 ASN A CG  1 
ATOM   1587 O OD1 . ASN A 1 199 ? 6.689   -6.104  -2.673  1.00 32.16 ? 200 ASN A OD1 1 
ATOM   1588 N ND2 . ASN A 1 199 ? 5.904   -8.017  -3.538  1.00 34.49 ? 200 ASN A ND2 1 
ATOM   1589 N N   . TYR A 1 200 ? 11.516  -7.169  -4.436  1.00 28.94 ? 201 TYR A N   1 
ATOM   1590 C CA  . TYR A 1 200 ? 12.808  -7.840  -4.476  1.00 31.86 ? 201 TYR A CA  1 
ATOM   1591 C C   . TYR A 1 200 ? 13.862  -6.884  -3.921  1.00 34.36 ? 201 TYR A C   1 
ATOM   1592 O O   . TYR A 1 200 ? 14.160  -5.854  -4.532  1.00 33.97 ? 201 TYR A O   1 
ATOM   1593 C CB  . TYR A 1 200 ? 13.104  -8.281  -5.911  1.00 32.06 ? 201 TYR A CB  1 
ATOM   1594 C CG  . TYR A 1 200 ? 14.366  -9.095  -6.166  1.00 36.98 ? 201 TYR A CG  1 
ATOM   1595 C CD1 . TYR A 1 200 ? 15.138  -9.602  -5.128  1.00 33.50 ? 201 TYR A CD1 1 
ATOM   1596 C CD2 . TYR A 1 200 ? 14.778  -9.355  -7.469  1.00 38.85 ? 201 TYR A CD2 1 
ATOM   1597 C CE1 . TYR A 1 200 ? 16.291  -10.322 -5.387  1.00 34.16 ? 201 TYR A CE1 1 
ATOM   1598 C CE2 . TYR A 1 200 ? 15.920  -10.078 -7.736  1.00 40.72 ? 201 TYR A CE2 1 
ATOM   1599 C CZ  . TYR A 1 200 ? 16.674  -10.561 -6.697  1.00 40.46 ? 201 TYR A CZ  1 
ATOM   1600 O OH  . TYR A 1 200 ? 17.815  -11.283 -6.977  1.00 38.68 ? 201 TYR A OH  1 
ATOM   1601 N N   . ALA A 1 201 ? 14.416  -7.221  -2.758  1.00 33.14 ? 202 ALA A N   1 
ATOM   1602 C CA  . ALA A 1 201 ? 15.423  -6.375  -2.125  1.00 32.89 ? 202 ALA A CA  1 
ATOM   1603 C C   . ALA A 1 201 ? 16.693  -6.298  -2.965  1.00 36.09 ? 202 ALA A C   1 
ATOM   1604 O O   . ALA A 1 201 ? 17.151  -7.300  -3.521  1.00 37.78 ? 202 ALA A O   1 
ATOM   1605 C CB  . ALA A 1 201 ? 15.774  -6.908  -0.734  1.00 29.04 ? 202 ALA A CB  1 
ATOM   1606 N N   . PHE A 1 202 ? 17.264  -5.098  -3.052  1.00 33.81 ? 203 PHE A N   1 
ATOM   1607 C CA  . PHE A 1 202 ? 18.609  -4.952  -3.594  1.00 39.79 ? 203 PHE A CA  1 
ATOM   1608 C C   . PHE A 1 202 ? 19.640  -5.470  -2.595  1.00 43.44 ? 203 PHE A C   1 
ATOM   1609 O O   . PHE A 1 202 ? 19.518  -5.245  -1.387  1.00 39.01 ? 203 PHE A O   1 
ATOM   1610 C CB  . PHE A 1 202 ? 18.911  -3.487  -3.908  1.00 43.95 ? 203 PHE A CB  1 
ATOM   1611 C CG  . PHE A 1 202 ? 18.164  -2.949  -5.085  1.00 44.94 ? 203 PHE A CG  1 
ATOM   1612 C CD1 . PHE A 1 202 ? 18.094  -3.671  -6.264  1.00 49.05 ? 203 PHE A CD1 1 
ATOM   1613 C CD2 . PHE A 1 202 ? 17.530  -1.713  -5.011  1.00 51.58 ? 203 PHE A CD2 1 
ATOM   1614 C CE1 . PHE A 1 202 ? 17.402  -3.171  -7.354  1.00 53.13 ? 203 PHE A CE1 1 
ATOM   1615 C CE2 . PHE A 1 202 ? 16.839  -1.204  -6.094  1.00 52.89 ? 203 PHE A CE2 1 
ATOM   1616 C CZ  . PHE A 1 202 ? 16.774  -1.938  -7.268  1.00 55.24 ? 203 PHE A CZ  1 
ATOM   1617 N N   . GLY A 1 203 ? 20.656  -6.171  -3.106  1.00 43.29 ? 204 GLY A N   1 
ATOM   1618 C CA  . GLY A 1 203 ? 21.842  -6.442  -2.309  1.00 46.39 ? 204 GLY A CA  1 
ATOM   1619 C C   . GLY A 1 203 ? 22.822  -5.282  -2.372  1.00 50.98 ? 204 GLY A C   1 
ATOM   1620 O O   . GLY A 1 203 ? 22.944  -4.597  -3.385  1.00 50.61 ? 204 GLY A O   1 
ATOM   1621 N N   . TYR A 1 204 ? 23.521  -5.046  -1.262  1.00 49.84 ? 205 TYR A N   1 
ATOM   1622 C CA  . TYR A 1 204 ? 24.427  -3.909  -1.137  1.00 45.97 ? 205 TYR A CA  1 
ATOM   1623 C C   . TYR A 1 204 ? 25.832  -4.398  -0.817  1.00 53.70 ? 205 TYR A C   1 
ATOM   1624 O O   . TYR A 1 204 ? 26.017  -5.200  0.105   1.00 48.96 ? 205 TYR A O   1 
ATOM   1625 C CB  . TYR A 1 204 ? 23.932  -2.931  -0.065  1.00 48.31 ? 205 TYR A CB  1 
ATOM   1626 C CG  . TYR A 1 204 ? 22.677  -2.224  -0.509  1.00 47.46 ? 205 TYR A CG  1 
ATOM   1627 C CD1 . TYR A 1 204 ? 21.433  -2.798  -0.297  1.00 43.11 ? 205 TYR A CD1 1 
ATOM   1628 C CD2 . TYR A 1 204 ? 22.739  -1.010  -1.190  1.00 44.99 ? 205 TYR A CD2 1 
ATOM   1629 C CE1 . TYR A 1 204 ? 20.281  -2.180  -0.717  1.00 41.50 ? 205 TYR A CE1 1 
ATOM   1630 C CE2 . TYR A 1 204 ? 21.589  -0.386  -1.620  1.00 45.43 ? 205 TYR A CE2 1 
ATOM   1631 C CZ  . TYR A 1 204 ? 20.359  -0.978  -1.379  1.00 41.73 ? 205 TYR A CZ  1 
ATOM   1632 O OH  . TYR A 1 204 ? 19.194  -0.378  -1.805  1.00 40.53 ? 205 TYR A OH  1 
ATOM   1633 N N   . ASN A 1 205 ? 26.814  -3.918  -1.585  1.00 55.30 ? 206 ASN A N   1 
ATOM   1634 C CA  . ASN A 1 205 ? 28.198  -4.353  -1.430  1.00 59.07 ? 206 ASN A CA  1 
ATOM   1635 C C   . ASN A 1 205 ? 28.848  -3.592  -0.277  1.00 61.10 ? 206 ASN A C   1 
ATOM   1636 O O   . ASN A 1 205 ? 28.203  -2.812  0.432   1.00 59.41 ? 206 ASN A O   1 
ATOM   1637 C CB  . ASN A 1 205 ? 28.969  -4.189  -2.744  1.00 58.00 ? 206 ASN A CB  1 
ATOM   1638 C CG  . ASN A 1 205 ? 29.040  -2.737  -3.230  1.00 59.93 ? 206 ASN A CG  1 
ATOM   1639 O OD1 . ASN A 1 205 ? 28.911  -1.787  -2.455  1.00 62.00 ? 206 ASN A OD1 1 
ATOM   1640 N ND2 . ASN A 1 205 ? 29.249  -2.569  -4.528  1.00 58.40 ? 206 ASN A ND2 1 
ATOM   1641 N N   . GLN A 1 206 ? 30.152  -3.797  -0.088  1.00 61.28 ? 207 GLN A N   1 
ATOM   1642 C CA  . GLN A 1 206 ? 30.843  -3.153  1.024   1.00 66.51 ? 207 GLN A CA  1 
ATOM   1643 C C   . GLN A 1 206 ? 30.952  -1.643  0.851   1.00 67.31 ? 207 GLN A C   1 
ATOM   1644 O O   . GLN A 1 206 ? 31.206  -0.939  1.835   1.00 66.58 ? 207 GLN A O   1 
ATOM   1645 C CB  . GLN A 1 206 ? 32.227  -3.779  1.209   1.00 69.61 ? 207 GLN A CB  1 
ATOM   1646 C CG  . GLN A 1 206 ? 32.166  -5.260  1.538   1.00 66.28 ? 207 GLN A CG  1 
ATOM   1647 C CD  . GLN A 1 206 ? 31.001  -5.605  2.458   1.00 67.68 ? 207 GLN A CD  1 
ATOM   1648 O OE1 . GLN A 1 206 ? 30.036  -6.249  2.042   1.00 64.54 ? 207 GLN A OE1 1 
ATOM   1649 N NE2 . GLN A 1 206 ? 31.085  -5.172  3.713   1.00 67.89 ? 207 GLN A NE2 1 
ATOM   1650 N N   . GLU A 1 207 ? 30.759  -1.127  -0.364  1.00 70.12 ? 208 GLU A N   1 
ATOM   1651 C CA  . GLU A 1 207 ? 30.650  0.309   -0.597  1.00 69.77 ? 208 GLU A CA  1 
ATOM   1652 C C   . GLU A 1 207 ? 29.204  0.792   -0.596  1.00 65.98 ? 208 GLU A C   1 
ATOM   1653 O O   . GLU A 1 207 ? 28.947  1.941   -0.971  1.00 71.28 ? 208 GLU A O   1 
ATOM   1654 C CB  . GLU A 1 207 ? 31.326  0.694   -1.918  1.00 72.86 ? 208 GLU A CB  1 
ATOM   1655 C CG  . GLU A 1 207 ? 32.838  0.874   -1.826  1.00 79.08 ? 208 GLU A CG  1 
ATOM   1656 C CD  . GLU A 1 207 ? 33.586  -0.440  -1.676  1.00 82.90 ? 208 GLU A CD  1 
ATOM   1657 O OE1 . GLU A 1 207 ? 33.125  -1.463  -2.233  1.00 79.52 ? 208 GLU A OE1 1 
ATOM   1658 O OE2 . GLU A 1 207 ? 34.637  -0.450  -0.997  1.00 85.62 ? 208 GLU A OE2 1 
ATOM   1659 N N   . ASN A 1 208 ? 28.264  -0.068  -0.196  1.00 62.84 ? 209 ASN A N   1 
ATOM   1660 C CA  . ASN A 1 208 ? 26.853  0.289   -0.020  1.00 61.14 ? 209 ASN A CA  1 
ATOM   1661 C C   . ASN A 1 208 ? 26.201  0.706   -1.337  1.00 57.63 ? 209 ASN A C   1 
ATOM   1662 O O   . ASN A 1 208 ? 25.341  1.587   -1.372  1.00 57.03 ? 209 ASN A O   1 
ATOM   1663 C CB  . ASN A 1 208 ? 26.686  1.377   1.045   1.00 63.34 ? 209 ASN A CB  1 
ATOM   1664 C CG  . ASN A 1 208 ? 27.387  1.029   2.349   1.00 62.97 ? 209 ASN A CG  1 
ATOM   1665 O OD1 . ASN A 1 208 ? 26.953  0.141   3.089   1.00 54.66 ? 209 ASN A OD1 1 
ATOM   1666 N ND2 . ASN A 1 208 ? 28.482  1.730   2.637   1.00 61.95 ? 209 ASN A ND2 1 
ATOM   1667 N N   . GLN A 1 209 ? 26.595  0.051   -2.431  1.00 58.80 ? 210 GLN A N   1 
ATOM   1668 C CA  . GLN A 1 209 ? 25.959  0.279   -3.720  1.00 58.16 ? 210 GLN A CA  1 
ATOM   1669 C C   . GLN A 1 209 ? 25.055  -0.895  -4.084  1.00 55.36 ? 210 GLN A C   1 
ATOM   1670 O O   . GLN A 1 209 ? 25.407  -2.049  -3.811  1.00 54.16 ? 210 GLN A O   1 
ATOM   1671 C CB  . GLN A 1 209 ? 27.006  0.473   -4.825  1.00 62.17 ? 210 GLN A CB  1 
ATOM   1672 C CG  . GLN A 1 209 ? 28.144  1.433   -4.464  1.00 63.42 ? 210 GLN A CG  1 
ATOM   1673 C CD  . GLN A 1 209 ? 27.665  2.836   -4.130  1.00 66.65 ? 210 GLN A CD  1 
ATOM   1674 O OE1 . GLN A 1 209 ? 26.600  3.271   -4.576  1.00 67.38 ? 210 GLN A OE1 1 
ATOM   1675 N NE2 . GLN A 1 209 ? 28.455  3.554   -3.336  1.00 67.57 ? 210 GLN A NE2 1 
ATOM   1676 N N   . PRO A 1 210 ? 23.897  -0.644  -4.703  1.00 55.30 ? 211 PRO A N   1 
ATOM   1677 C CA  . PRO A 1 210 ? 22.985  -1.750  -5.033  1.00 54.62 ? 211 PRO A CA  1 
ATOM   1678 C C   . PRO A 1 210 ? 23.548  -2.612  -6.154  1.00 56.81 ? 211 PRO A C   1 
ATOM   1679 O O   . PRO A 1 210 ? 24.056  -2.102  -7.154  1.00 60.39 ? 211 PRO A O   1 
ATOM   1680 C CB  . PRO A 1 210 ? 21.703  -1.033  -5.470  1.00 53.16 ? 211 PRO A CB  1 
ATOM   1681 C CG  . PRO A 1 210 ? 22.190  0.269   -6.021  1.00 54.24 ? 211 PRO A CG  1 
ATOM   1682 C CD  . PRO A 1 210 ? 23.382  0.655   -5.176  1.00 53.71 ? 211 PRO A CD  1 
ATOM   1683 N N   . ILE A 1 211 ? 23.445  -3.930  -5.984  1.00 56.06 ? 212 ILE A N   1 
ATOM   1684 C CA  . ILE A 1 211 ? 24.046  -4.886  -6.910  1.00 58.53 ? 212 ILE A CA  1 
ATOM   1685 C C   . ILE A 1 211 ? 23.071  -6.030  -7.167  1.00 62.34 ? 212 ILE A C   1 
ATOM   1686 O O   . ILE A 1 211 ? 22.535  -6.626  -6.225  1.00 57.30 ? 212 ILE A O   1 
ATOM   1687 C CB  . ILE A 1 211 ? 25.387  -5.431  -6.378  1.00 61.40 ? 212 ILE A CB  1 
ATOM   1688 C CG1 . ILE A 1 211 ? 26.506  -4.413  -6.622  1.00 58.38 ? 212 ILE A CG1 1 
ATOM   1689 C CG2 . ILE A 1 211 ? 25.714  -6.776  -7.014  1.00 63.69 ? 212 ILE A CG2 1 
ATOM   1690 C CD1 . ILE A 1 211 ? 27.905  -4.974  -6.423  1.00 64.77 ? 212 ILE A CD1 1 
ATOM   1691 N N   . ARG A 1 212 ? 22.847  -6.334  -8.446  1.00 61.20 ? 213 ARG A N   1 
ATOM   1692 C CA  . ARG A 1 212 ? 22.024  -7.458  -8.871  1.00 63.99 ? 213 ARG A CA  1 
ATOM   1693 C C   . ARG A 1 212 ? 22.715  -8.145  -10.038 1.00 64.42 ? 213 ARG A C   1 
ATOM   1694 O O   . ARG A 1 212 ? 23.146  -7.476  -10.982 1.00 64.13 ? 213 ARG A O   1 
ATOM   1695 C CB  . ARG A 1 212 ? 20.616  -6.995  -9.273  1.00 62.83 ? 213 ARG A CB  1 
ATOM   1696 C CG  . ARG A 1 212 ? 19.658  -8.129  -9.635  1.00 63.64 ? 213 ARG A CG  1 
ATOM   1697 C CD  . ARG A 1 212 ? 18.216  -7.658  -9.562  1.00 60.16 ? 213 ARG A CD  1 
ATOM   1698 N NE  . ARG A 1 212 ? 17.837  -7.335  -8.191  1.00 58.70 ? 213 ARG A NE  1 
ATOM   1699 C CZ  . ARG A 1 212 ? 16.785  -6.603  -7.852  1.00 50.52 ? 213 ARG A CZ  1 
ATOM   1700 N NH1 . ARG A 1 212 ? 15.992  -6.064  -8.766  1.00 58.07 ? 213 ARG A NH1 1 
ATOM   1701 N NH2 . ARG A 1 212 ? 16.525  -6.400  -6.563  1.00 42.61 ? 213 ARG A NH2 1 
ATOM   1702 N N   . VAL A 1 213 ? 22.830  -9.471  -9.972  1.00 66.48 ? 214 VAL A N   1 
ATOM   1703 C CA  . VAL A 1 213 ? 23.477  -10.251 -11.022 1.00 68.44 ? 214 VAL A CA  1 
ATOM   1704 C C   . VAL A 1 213 ? 22.710  -11.552 -11.218 1.00 67.81 ? 214 VAL A C   1 
ATOM   1705 O O   . VAL A 1 213 ? 22.160  -12.115 -10.265 1.00 61.81 ? 214 VAL A O   1 
ATOM   1706 C CB  . VAL A 1 213 ? 24.963  -10.537 -10.703 1.00 67.51 ? 214 VAL A CB  1 
ATOM   1707 C CG1 . VAL A 1 213 ? 25.098  -11.521 -9.552  1.00 66.43 ? 214 VAL A CG1 1 
ATOM   1708 C CG2 . VAL A 1 213 ? 25.692  -11.057 -11.941 1.00 65.12 ? 214 VAL A CG2 1 
ATOM   1709 N N   . ASN A 1 214 ? 22.657  -12.015 -12.461 1.00 69.49 ? 215 ASN A N   1 
ATOM   1710 C CA  . ASN A 1 214 ? 22.159  -13.348 -12.745 1.00 72.17 ? 215 ASN A CA  1 
ATOM   1711 C C   . ASN A 1 214 ? 23.217  -14.382 -12.362 1.00 66.97 ? 215 ASN A C   1 
ATOM   1712 O O   . ASN A 1 214 ? 24.410  -14.066 -12.283 1.00 59.98 ? 215 ASN A O   1 
ATOM   1713 C CB  . ASN A 1 214 ? 21.779  -13.465 -14.222 1.00 74.47 ? 215 ASN A CB  1 
ATOM   1714 C CG  . ASN A 1 214 ? 20.285  -13.262 -14.461 1.00 77.74 ? 215 ASN A CG  1 
ATOM   1715 O OD1 . ASN A 1 214 ? 19.455  -13.645 -13.634 1.00 78.39 ? 215 ASN A OD1 1 
ATOM   1716 N ND2 . ASN A 1 214 ? 19.940  -12.657 -15.594 1.00 80.60 ? 215 ASN A ND2 1 
ATOM   1717 N N   . PRO A 1 215 ? 22.808  -15.620 -12.086 1.00 67.26 ? 216 PRO A N   1 
ATOM   1718 C CA  . PRO A 1 215 ? 23.774  -16.618 -11.620 1.00 62.65 ? 216 PRO A CA  1 
ATOM   1719 C C   . PRO A 1 215 ? 24.746  -17.006 -12.719 1.00 61.05 ? 216 PRO A C   1 
ATOM   1720 O O   . PRO A 1 215 ? 24.479  -16.860 -13.914 1.00 61.70 ? 216 PRO A O   1 
ATOM   1721 C CB  . PRO A 1 215 ? 22.895  -17.807 -11.209 1.00 55.80 ? 216 PRO A CB  1 
ATOM   1722 C CG  . PRO A 1 215 ? 21.657  -17.650 -12.013 1.00 67.72 ? 216 PRO A CG  1 
ATOM   1723 C CD  . PRO A 1 215 ? 21.440  -16.168 -12.141 1.00 69.29 ? 216 PRO A CD  1 
ATOM   1724 N N   . GLY A 1 216 ? 25.910  -17.489 -12.287 1.00 51.06 ? 217 GLY A N   1 
ATOM   1725 C CA  . GLY A 1 216 ? 26.834  -18.107 -13.187 1.00 42.41 ? 217 GLY A CA  1 
ATOM   1726 C C   . GLY A 1 216 ? 26.363  -19.491 -13.582 1.00 37.56 ? 217 GLY A C   1 
ATOM   1727 O O   . GLY A 1 216 ? 25.293  -19.957 -13.166 1.00 37.17 ? 217 GLY A O   1 
ATOM   1728 N N   . PRO A 1 217 ? 27.160  -20.170 -14.398 1.00 35.86 ? 218 PRO A N   1 
ATOM   1729 C CA  . PRO A 1 217 ? 26.767  -21.518 -14.833 1.00 31.91 ? 218 PRO A CA  1 
ATOM   1730 C C   . PRO A 1 217 ? 26.731  -22.472 -13.646 1.00 30.59 ? 218 PRO A C   1 
ATOM   1731 O O   . PRO A 1 217 ? 27.616  -22.453 -12.788 1.00 32.95 ? 218 PRO A O   1 
ATOM   1732 C CB  . PRO A 1 217 ? 27.846  -21.893 -15.857 1.00 32.24 ? 218 PRO A CB  1 
ATOM   1733 C CG  . PRO A 1 217 ? 29.025  -21.045 -15.510 1.00 36.30 ? 218 PRO A CG  1 
ATOM   1734 C CD  . PRO A 1 217 ? 28.487  -19.773 -14.898 1.00 35.10 ? 218 PRO A CD  1 
ATOM   1735 N N   . LEU A 1 218 ? 25.666  -23.277 -13.588 1.00 29.69 ? 219 LEU A N   1 
ATOM   1736 C CA  . LEU A 1 218 ? 25.362  -24.161 -12.460 1.00 28.24 ? 219 LEU A CA  1 
ATOM   1737 C C   . LEU A 1 218 ? 25.306  -23.409 -11.134 1.00 25.33 ? 219 LEU A C   1 
ATOM   1738 O O   . LEU A 1 218 ? 25.538  -23.992 -10.071 1.00 25.81 ? 219 LEU A O   1 
ATOM   1739 C CB  . LEU A 1 218 ? 26.355  -25.333 -12.362 1.00 29.20 ? 219 LEU A CB  1 
ATOM   1740 C CG  . LEU A 1 218 ? 25.923  -26.671 -12.964 1.00 30.07 ? 219 LEU A CG  1 
ATOM   1741 C CD1 . LEU A 1 218 ? 25.548  -26.465 -14.424 1.00 37.48 ? 219 LEU A CD1 1 
ATOM   1742 C CD2 . LEU A 1 218 ? 27.027  -27.706 -12.849 1.00 25.49 ? 219 LEU A CD2 1 
ATOM   1743 N N   . GLY A 1 219 ? 24.967  -22.120 -11.179 1.00 28.09 ? 220 GLY A N   1 
ATOM   1744 C CA  . GLY A 1 219 ? 24.926  -21.336 -9.962  1.00 28.09 ? 220 GLY A CA  1 
ATOM   1745 C C   . GLY A 1 219 ? 23.656  -21.494 -9.154  1.00 26.14 ? 220 GLY A C   1 
ATOM   1746 O O   . GLY A 1 219 ? 23.693  -21.392 -7.923  1.00 25.18 ? 220 GLY A O   1 
ATOM   1747 N N   . ALA A 1 220 ? 22.524  -21.746 -9.815  1.00 25.26 ? 221 ALA A N   1 
ATOM   1748 C CA  . ALA A 1 220 ? 21.251  -21.782 -9.091  1.00 21.69 ? 221 ALA A CA  1 
ATOM   1749 C C   . ALA A 1 220 ? 21.225  -22.814 -7.960  1.00 23.80 ? 221 ALA A C   1 
ATOM   1750 O O   . ALA A 1 220 ? 20.773  -22.464 -6.853  1.00 23.00 ? 221 ALA A O   1 
ATOM   1751 C CB  . ALA A 1 220 ? 20.108  -21.983 -10.092 1.00 22.04 ? 221 ALA A CB  1 
ATOM   1752 N N   . PRO A 1 221 ? 21.694  -24.060 -8.130  1.00 19.28 ? 222 PRO A N   1 
ATOM   1753 C CA  . PRO A 1 221 ? 21.683  -24.995 -6.988  1.00 18.63 ? 222 PRO A CA  1 
ATOM   1754 C C   . PRO A 1 221 ? 22.593  -24.572 -5.836  1.00 21.94 ? 222 PRO A C   1 
ATOM   1755 O O   . PRO A 1 221 ? 22.425  -25.080 -4.715  1.00 19.81 ? 222 PRO A O   1 
ATOM   1756 C CB  . PRO A 1 221 ? 22.162  -26.320 -7.603  1.00 21.17 ? 222 PRO A CB  1 
ATOM   1757 C CG  . PRO A 1 221 ? 21.996  -26.164 -9.083  1.00 20.85 ? 222 PRO A CG  1 
ATOM   1758 C CD  . PRO A 1 221 ? 22.228  -24.707 -9.343  1.00 20.29 ? 222 PRO A CD  1 
ATOM   1759 N N   . ALA A 1 222 ? 23.545  -23.664 -6.064  1.00 20.78 ? 223 ALA A N   1 
ATOM   1760 C CA  . ALA A 1 222 ? 24.496  -23.293 -5.015  1.00 21.14 ? 223 ALA A CA  1 
ATOM   1761 C C   . ALA A 1 222 ? 24.104  -22.014 -4.277  1.00 23.19 ? 223 ALA A C   1 
ATOM   1762 O O   . ALA A 1 222 ? 24.309  -21.920 -3.062  1.00 21.48 ? 223 ALA A O   1 
ATOM   1763 C CB  . ALA A 1 222 ? 25.908  -23.142 -5.614  1.00 21.44 ? 223 ALA A CB  1 
ATOM   1764 N N   . TYR A 1 223 ? 23.505  -21.044 -4.981  1.00 20.45 ? 224 TYR A N   1 
ATOM   1765 C CA  . TYR A 1 223 ? 23.163  -19.764 -4.365  1.00 22.72 ? 224 TYR A CA  1 
ATOM   1766 C C   . TYR A 1 223 ? 22.002  -19.042 -5.051  1.00 24.03 ? 224 TYR A C   1 
ATOM   1767 O O   . TYR A 1 223 ? 21.892  -17.821 -4.905  1.00 25.40 ? 224 TYR A O   1 
ATOM   1768 C CB  . TYR A 1 223 ? 24.389  -18.822 -4.382  1.00 23.98 ? 224 TYR A CB  1 
ATOM   1769 C CG  . TYR A 1 223 ? 25.037  -18.733 -5.748  1.00 24.78 ? 224 TYR A CG  1 
ATOM   1770 C CD1 . TYR A 1 223 ? 24.500  -17.919 -6.738  1.00 31.55 ? 224 TYR A CD1 1 
ATOM   1771 C CD2 . TYR A 1 223 ? 26.171  -19.482 -6.055  1.00 27.89 ? 224 TYR A CD2 1 
ATOM   1772 C CE1 . TYR A 1 223 ? 25.084  -17.837 -7.998  1.00 37.00 ? 224 TYR A CE1 1 
ATOM   1773 C CE2 . TYR A 1 223 ? 26.763  -19.406 -7.318  1.00 33.09 ? 224 TYR A CE2 1 
ATOM   1774 C CZ  . TYR A 1 223 ? 26.207  -18.583 -8.279  1.00 34.82 ? 224 TYR A CZ  1 
ATOM   1775 O OH  . TYR A 1 223 ? 26.766  -18.493 -9.532  1.00 44.98 ? 224 TYR A OH  1 
ATOM   1776 N N   . GLY A 1 224 ? 21.120  -19.736 -5.764  1.00 25.12 ? 225 GLY A N   1 
ATOM   1777 C CA  . GLY A 1 224 ? 20.197  -19.057 -6.648  1.00 24.16 ? 225 GLY A CA  1 
ATOM   1778 C C   . GLY A 1 224 ? 18.784  -18.831 -6.153  1.00 24.40 ? 225 GLY A C   1 
ATOM   1779 O O   . GLY A 1 224 ? 17.949  -18.389 -6.949  1.00 25.15 ? 225 GLY A O   1 
ATOM   1780 N N   . VAL A 1 225 ? 18.476  -19.094 -4.871  1.00 19.89 ? 226 VAL A N   1 
ATOM   1781 C CA  . VAL A 1 225 ? 17.102  -18.980 -4.378  1.00 20.16 ? 226 VAL A CA  1 
ATOM   1782 C C   . VAL A 1 225 ? 16.910  -17.643 -3.669  1.00 20.67 ? 226 VAL A C   1 
ATOM   1783 O O   . VAL A 1 225 ? 17.816  -17.151 -3.002  1.00 18.87 ? 226 VAL A O   1 
ATOM   1784 C CB  . VAL A 1 225 ? 16.746  -20.157 -3.451  1.00 18.14 ? 226 VAL A CB  1 
ATOM   1785 C CG1 . VAL A 1 225 ? 15.339  -19.981 -2.853  1.00 18.65 ? 226 VAL A CG1 1 
ATOM   1786 C CG2 . VAL A 1 225 ? 16.855  -21.468 -4.231  1.00 20.24 ? 226 VAL A CG2 1 
ATOM   1787 N N   . LYS A 1 226 ? 15.713  -17.070 -3.806  1.00 20.81 ? 227 LYS A N   1 
ATOM   1788 C CA  . LYS A 1 226 ? 15.284  -15.868 -3.100  1.00 22.82 ? 227 LYS A CA  1 
ATOM   1789 C C   . LYS A 1 226 ? 13.973  -16.189 -2.399  1.00 22.52 ? 227 LYS A C   1 
ATOM   1790 O O   . LYS A 1 226 ? 13.149  -16.932 -2.940  1.00 27.13 ? 227 LYS A O   1 
ATOM   1791 C CB  . LYS A 1 226 ? 15.079  -14.676 -4.065  1.00 23.81 ? 227 LYS A CB  1 
ATOM   1792 C CG  . LYS A 1 226 ? 16.274  -14.294 -4.940  1.00 24.18 ? 227 LYS A CG  1 
ATOM   1793 C CD  . LYS A 1 226 ? 16.366  -15.162 -6.205  1.00 29.05 ? 227 LYS A CD  1 
ATOM   1794 C CE  . LYS A 1 226 ? 17.424  -14.637 -7.175  1.00 29.55 ? 227 LYS A CE  1 
ATOM   1795 N NZ  . LYS A 1 226 ? 17.914  -15.723 -8.065  1.00 33.03 ? 227 LYS A NZ  1 
ATOM   1796 N N   . SER A 1 227 ? 13.766  -15.630 -1.208  1.00 22.23 ? 228 SER A N   1 
ATOM   1797 C CA  . SER A 1 227 ? 12.558  -15.960 -0.463  1.00 22.94 ? 228 SER A CA  1 
ATOM   1798 C C   . SER A 1 227 ? 12.222  -14.828 0.506   1.00 22.15 ? 228 SER A C   1 
ATOM   1799 O O   . SER A 1 227 ? 13.030  -13.928 0.744   1.00 21.84 ? 228 SER A O   1 
ATOM   1800 C CB  . SER A 1 227 ? 12.732  -17.294 0.273   1.00 18.56 ? 228 SER A CB  1 
ATOM   1801 O OG  . SER A 1 227 ? 11.539  -17.646 0.927   1.00 23.83 ? 228 SER A OG  1 
ATOM   1802 N N   . THR A 1 228 ? 10.995  -14.878 1.041   1.00 23.36 ? 229 THR A N   1 
ATOM   1803 C CA  . THR A 1 228 ? 10.512  -13.962 2.070   1.00 21.54 ? 229 THR A CA  1 
ATOM   1804 C C   . THR A 1 228 ? 10.704  -14.579 3.457   1.00 22.62 ? 229 THR A C   1 
ATOM   1805 O O   . THR A 1 228 ? 10.940  -15.786 3.598   1.00 21.99 ? 229 THR A O   1 
ATOM   1806 C CB  . THR A 1 228 ? 9.020   -13.636 1.880   1.00 21.55 ? 229 THR A CB  1 
ATOM   1807 O OG1 . THR A 1 228 ? 8.245   -14.813 2.140   1.00 21.96 ? 229 THR A OG1 1 
ATOM   1808 C CG2 . THR A 1 228 ? 8.723   -13.134 0.463   1.00 23.07 ? 229 THR A CG2 1 
ATOM   1809 N N   . LEU A 1 229 ? 10.598  -13.738 4.494   1.00 19.68 ? 230 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 229 ? 10.657  -14.260 5.859   1.00 20.46 ? 230 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 229 ? 9.492   -15.188 6.190   1.00 19.98 ? 230 LEU A C   1 
ATOM   1812 O O   . LEU A 1 229 ? 9.747   -16.256 6.769   1.00 21.78 ? 230 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 229 ? 10.751  -13.118 6.888   1.00 21.38 ? 230 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 229 ? 10.867  -13.597 8.354   1.00 22.41 ? 230 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 229 ? 12.162  -14.385 8.587   1.00 22.71 ? 230 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 229 ? 10.759  -12.440 9.380   1.00 21.60 ? 230 LEU A CD2 1 
ATOM   1817 N N   . PRO A 1 230 ? 8.228   -14.882 5.853   1.00 20.82 ? 231 PRO A N   1 
ATOM   1818 C CA  . PRO A 1 230 ? 7.169   -15.868 6.140   1.00 22.78 ? 231 PRO A CA  1 
ATOM   1819 C C   . PRO A 1 230 ? 7.410   -17.216 5.472   1.00 20.89 ? 231 PRO A C   1 
ATOM   1820 O O   . PRO A 1 230 ? 7.171   -18.264 6.095   1.00 24.19 ? 231 PRO A O   1 
ATOM   1821 C CB  . PRO A 1 230 ? 5.902   -15.187 5.607   1.00 25.52 ? 231 PRO A CB  1 
ATOM   1822 C CG  . PRO A 1 230 ? 6.185   -13.710 5.726   1.00 23.24 ? 231 PRO A CG  1 
ATOM   1823 C CD  . PRO A 1 230 ? 7.673   -13.600 5.379   1.00 22.82 ? 231 PRO A CD  1 
ATOM   1824 N N   . ASP A 1 231 ? 7.882   -17.223 4.220   1.00 20.19 ? 232 ASP A N   1 
ATOM   1825 C CA  . ASP A 1 231 ? 8.182   -18.489 3.548   1.00 20.58 ? 232 ASP A CA  1 
ATOM   1826 C C   . ASP A 1 231 ? 9.299   -19.248 4.248   1.00 21.03 ? 232 ASP A C   1 
ATOM   1827 O O   . ASP A 1 231 ? 9.243   -20.487 4.373   1.00 19.14 ? 232 ASP A O   1 
ATOM   1828 C CB  . ASP A 1 231 ? 8.586   -18.252 2.097   1.00 19.44 ? 232 ASP A CB  1 
ATOM   1829 C CG  . ASP A 1 231 ? 7.405   -18.189 1.169   1.00 24.49 ? 232 ASP A CG  1 
ATOM   1830 O OD1 . ASP A 1 231 ? 6.271   -18.049 1.669   1.00 28.25 ? 232 ASP A OD1 1 
ATOM   1831 O OD2 . ASP A 1 231 ? 7.615   -18.253 -0.057  1.00 27.41 ? 232 ASP A OD2 1 
ATOM   1832 N N   . MET A 1 232 ? 10.358  -18.540 4.655   1.00 19.78 ? 233 MET A N   1 
ATOM   1833 C CA  . MET A 1 232 ? 11.459  -19.242 5.314   1.00 19.45 ? 233 MET A CA  1 
ATOM   1834 C C   . MET A 1 232 ? 11.036  -19.798 6.671   1.00 20.74 ? 233 MET A C   1 
ATOM   1835 O O   . MET A 1 232 ? 11.509  -20.871 7.065   1.00 21.49 ? 233 MET A O   1 
ATOM   1836 C CB  . MET A 1 232 ? 12.686  -18.326 5.441   1.00 21.09 ? 233 MET A CB  1 
ATOM   1837 C CG  . MET A 1 232 ? 13.444  -18.063 4.102   1.00 19.89 ? 233 MET A CG  1 
ATOM   1838 S SD  . MET A 1 232 ? 13.876  -19.602 3.203   1.00 21.51 ? 233 MET A SD  1 
ATOM   1839 C CE  . MET A 1 232 ? 15.159  -20.267 4.250   1.00 21.14 ? 233 MET A CE  1 
ATOM   1840 N N   . LEU A 1 233 ? 10.144  -19.101 7.397   1.00 21.07 ? 234 LEU A N   1 
ATOM   1841 C CA  . LEU A 1 233 ? 9.620   -19.672 8.639   1.00 22.97 ? 234 LEU A CA  1 
ATOM   1842 C C   . LEU A 1 233 ? 8.790   -20.923 8.368   1.00 21.57 ? 234 LEU A C   1 
ATOM   1843 O O   . LEU A 1 233 ? 8.835   -21.880 9.150   1.00 21.01 ? 234 LEU A O   1 
ATOM   1844 C CB  . LEU A 1 233 ? 8.797   -18.637 9.405   1.00 20.84 ? 234 LEU A CB  1 
ATOM   1845 C CG  . LEU A 1 233 ? 9.623   -17.484 9.989   1.00 20.95 ? 234 LEU A CG  1 
ATOM   1846 C CD1 . LEU A 1 233 ? 8.741   -16.448 10.676  1.00 24.16 ? 234 LEU A CD1 1 
ATOM   1847 C CD2 . LEU A 1 233 ? 10.687  -18.026 10.958  1.00 22.56 ? 234 LEU A CD2 1 
ATOM   1848 N N   . SER A 1 234 ? 8.007   -20.935 7.280   1.00 19.82 ? 235 SER A N   1 
ATOM   1849 C CA  . SER A 1 234 ? 7.304   -22.165 6.910   1.00 20.89 ? 235 SER A CA  1 
ATOM   1850 C C   . SER A 1 234 ? 8.283   -23.295 6.616   1.00 20.52 ? 235 SER A C   1 
ATOM   1851 O O   . SER A 1 234 ? 8.040   -24.454 6.982   1.00 19.79 ? 235 SER A O   1 
ATOM   1852 C CB  . SER A 1 234 ? 6.400   -21.936 5.692   1.00 23.16 ? 235 SER A CB  1 
ATOM   1853 O OG  . SER A 1 234 ? 5.286   -21.132 6.020   1.00 31.92 ? 235 SER A OG  1 
ATOM   1854 N N   . PHE A 1 235 ? 9.381   -22.986 5.920   1.00 19.49 ? 236 PHE A N   1 
ATOM   1855 C CA  . PHE A 1 235 ? 10.375  -24.014 5.611   1.00 21.53 ? 236 PHE A CA  1 
ATOM   1856 C C   . PHE A 1 235 ? 10.978  -24.592 6.886   1.00 21.11 ? 236 PHE A C   1 
ATOM   1857 O O   . PHE A 1 235 ? 11.195  -25.810 6.985   1.00 17.06 ? 236 PHE A O   1 
ATOM   1858 C CB  . PHE A 1 235 ? 11.465  -23.437 4.695   1.00 18.29 ? 236 PHE A CB  1 
ATOM   1859 C CG  . PHE A 1 235 ? 12.551  -24.439 4.320   1.00 17.54 ? 236 PHE A CG  1 
ATOM   1860 C CD1 . PHE A 1 235 ? 12.241  -25.615 3.643   1.00 19.57 ? 236 PHE A CD1 1 
ATOM   1861 C CD2 . PHE A 1 235 ? 13.878  -24.196 4.652   1.00 20.48 ? 236 PHE A CD2 1 
ATOM   1862 C CE1 . PHE A 1 235 ? 13.226  -26.538 3.308   1.00 20.32 ? 236 PHE A CE1 1 
ATOM   1863 C CE2 . PHE A 1 235 ? 14.880  -25.114 4.313   1.00 19.55 ? 236 PHE A CE2 1 
ATOM   1864 C CZ  . PHE A 1 235 ? 14.552  -26.282 3.641   1.00 21.22 ? 236 PHE A CZ  1 
ATOM   1865 N N   . ILE A 1 236 ? 11.226  -23.741 7.888   1.00 18.48 ? 237 ILE A N   1 
ATOM   1866 C CA  . ILE A 1 236 ? 11.763  -24.242 9.153   1.00 20.80 ? 237 ILE A CA  1 
ATOM   1867 C C   . ILE A 1 236 ? 10.718  -25.084 9.873   1.00 21.28 ? 237 ILE A C   1 
ATOM   1868 O O   . ILE A 1 236 ? 11.038  -26.121 10.477  1.00 21.43 ? 237 ILE A O   1 
ATOM   1869 C CB  . ILE A 1 236 ? 12.259  -23.078 10.038  1.00 19.49 ? 237 ILE A CB  1 
ATOM   1870 C CG1 . ILE A 1 236 ? 13.395  -22.298 9.363   1.00 23.82 ? 237 ILE A CG1 1 
ATOM   1871 C CG2 . ILE A 1 236 ? 12.659  -23.587 11.435  1.00 19.37 ? 237 ILE A CG2 1 
ATOM   1872 C CD1 . ILE A 1 236 ? 14.676  -23.070 9.070   1.00 27.03 ? 237 ILE A CD1 1 
ATOM   1873 N N   . HIS A 1 237 ? 9.449   -24.667 9.801   1.00 18.26 ? 238 HIS A N   1 
ATOM   1874 C CA  . HIS A 1 237 ? 8.368   -25.475 10.360  1.00 21.55 ? 238 HIS A CA  1 
ATOM   1875 C C   . HIS A 1 237 ? 8.325   -26.867 9.734   1.00 18.60 ? 238 HIS A C   1 
ATOM   1876 O O   . HIS A 1 237 ? 8.139   -27.868 10.439  1.00 19.94 ? 238 HIS A O   1 
ATOM   1877 C CB  . HIS A 1 237 ? 7.025   -24.770 10.149  1.00 22.37 ? 238 HIS A CB  1 
ATOM   1878 C CG  . HIS A 1 237 ? 5.843   -25.597 10.550  1.00 25.66 ? 238 HIS A CG  1 
ATOM   1879 N ND1 . HIS A 1 237 ? 5.572   -25.903 11.865  1.00 28.64 ? 238 HIS A ND1 1 
ATOM   1880 C CD2 . HIS A 1 237 ? 4.859   -26.175 9.817   1.00 24.44 ? 238 HIS A CD2 1 
ATOM   1881 C CE1 . HIS A 1 237 ? 4.475   -26.639 11.927  1.00 33.09 ? 238 HIS A CE1 1 
ATOM   1882 N NE2 . HIS A 1 237 ? 4.020   -26.811 10.699  1.00 27.67 ? 238 HIS A NE2 1 
ATOM   1883 N N   . ALA A 1 238 ? 8.480   -26.950 8.410   1.00 18.18 ? 239 ALA A N   1 
ATOM   1884 C CA  . ALA A 1 238 ? 8.485   -28.259 7.757   1.00 20.39 ? 239 ALA A CA  1 
ATOM   1885 C C   . ALA A 1 238 ? 9.653   -29.112 8.230   1.00 19.79 ? 239 ALA A C   1 
ATOM   1886 O O   . ALA A 1 238 ? 9.523   -30.335 8.355   1.00 17.97 ? 239 ALA A O   1 
ATOM   1887 C CB  . ALA A 1 238 ? 8.537   -28.094 6.236   1.00 18.70 ? 239 ALA A CB  1 
ATOM   1888 N N   . ASN A 1 239 ? 10.799  -28.488 8.504   1.00 17.51 ? 240 ASN A N   1 
ATOM   1889 C CA  . ASN A 1 239 ? 11.930  -29.246 9.032   1.00 19.44 ? 240 ASN A CA  1 
ATOM   1890 C C   . ASN A 1 239 ? 11.729  -29.650 10.493  1.00 20.01 ? 240 ASN A C   1 
ATOM   1891 O O   . ASN A 1 239 ? 12.254  -30.690 10.925  1.00 18.70 ? 240 ASN A O   1 
ATOM   1892 C CB  . ASN A 1 239 ? 13.213  -28.432 8.867   1.00 18.25 ? 240 ASN A CB  1 
ATOM   1893 C CG  . ASN A 1 239 ? 13.838  -28.615 7.503   1.00 19.88 ? 240 ASN A CG  1 
ATOM   1894 O OD1 . ASN A 1 239 ? 14.636  -29.525 7.308   1.00 21.95 ? 240 ASN A OD1 1 
ATOM   1895 N ND2 . ASN A 1 239 ? 13.466  -27.762 6.542   1.00 18.56 ? 240 ASN A ND2 1 
ATOM   1896 N N   . LEU A 1 240 ? 11.003  -28.838 11.270  1.00 20.04 ? 241 LEU A N   1 
ATOM   1897 C CA  . LEU A 1 240 ? 10.692  -29.179 12.656  1.00 22.05 ? 241 LEU A CA  1 
ATOM   1898 C C   . LEU A 1 240 ? 9.608   -30.250 12.764  1.00 24.32 ? 241 LEU A C   1 
ATOM   1899 O O   . LEU A 1 240 ? 9.620   -31.055 13.708  1.00 22.16 ? 241 LEU A O   1 
ATOM   1900 C CB  . LEU A 1 240 ? 10.251  -27.925 13.423  1.00 22.41 ? 241 LEU A CB  1 
ATOM   1901 C CG  . LEU A 1 240 ? 11.335  -26.929 13.847  1.00 23.95 ? 241 LEU A CG  1 
ATOM   1902 C CD1 . LEU A 1 240 ? 10.734  -25.565 14.216  1.00 20.02 ? 241 LEU A CD1 1 
ATOM   1903 C CD2 . LEU A 1 240 ? 12.148  -27.473 15.022  1.00 20.77 ? 241 LEU A CD2 1 
ATOM   1904 N N   . ASN A 1 241 ? 8.665   -30.291 11.825  1.00 22.92 ? 242 ASN A N   1 
ATOM   1905 C CA  . ASN A 1 241 ? 7.538   -31.223 11.917  1.00 23.78 ? 242 ASN A CA  1 
ATOM   1906 C C   . ASN A 1 241 ? 7.254   -31.861 10.566  1.00 23.69 ? 242 ASN A C   1 
ATOM   1907 O O   . ASN A 1 241 ? 6.163   -31.704 10.007  1.00 22.99 ? 242 ASN A O   1 
ATOM   1908 C CB  . ASN A 1 241 ? 6.301   -30.506 12.454  1.00 24.70 ? 242 ASN A CB  1 
ATOM   1909 C CG  . ASN A 1 241 ? 6.441   -30.155 13.916  1.00 34.56 ? 242 ASN A CG  1 
ATOM   1910 O OD1 . ASN A 1 241 ? 6.306   -31.024 14.776  1.00 37.64 ? 242 ASN A OD1 1 
ATOM   1911 N ND2 . ASN A 1 241 ? 6.738   -28.890 14.208  1.00 35.46 ? 242 ASN A ND2 1 
ATOM   1912 N N   . PRO A 1 242 ? 8.212   -32.619 10.022  1.00 20.75 ? 243 PRO A N   1 
ATOM   1913 C CA  . PRO A 1 242 ? 7.985   -33.214 8.694   1.00 22.92 ? 243 PRO A CA  1 
ATOM   1914 C C   . PRO A 1 242 ? 6.823   -34.184 8.667   1.00 24.05 ? 243 PRO A C   1 
ATOM   1915 O O   . PRO A 1 242 ? 6.200   -34.356 7.610   1.00 23.19 ? 243 PRO A O   1 
ATOM   1916 C CB  . PRO A 1 242 ? 9.320   -33.908 8.381   1.00 21.28 ? 243 PRO A CB  1 
ATOM   1917 C CG  . PRO A 1 242 ? 10.019  -34.042 9.682   1.00 22.44 ? 243 PRO A CG  1 
ATOM   1918 C CD  . PRO A 1 242 ? 9.558   -32.924 10.545  1.00 21.42 ? 243 PRO A CD  1 
ATOM   1919 N N   . GLN A 1 243 ? 6.497   -34.809 9.804   1.00 21.69 ? 244 GLN A N   1 
ATOM   1920 C CA  . GLN A 1 243 ? 5.406   -35.778 9.848   1.00 25.19 ? 244 GLN A CA  1 
ATOM   1921 C C   . GLN A 1 243 ? 4.048   -35.148 9.540   1.00 25.13 ? 244 GLN A C   1 
ATOM   1922 O O   . GLN A 1 243 ? 3.090   -35.883 9.273   1.00 28.18 ? 244 GLN A O   1 
ATOM   1923 C CB  . GLN A 1 243 ? 5.377   -36.487 11.221  1.00 24.89 ? 244 GLN A CB  1 
ATOM   1924 C CG  . GLN A 1 243 ? 4.842   -35.647 12.402  1.00 26.67 ? 244 GLN A CG  1 
ATOM   1925 C CD  . GLN A 1 243 ? 5.820   -34.571 12.906  1.00 26.59 ? 244 GLN A CD  1 
ATOM   1926 O OE1 . GLN A 1 243 ? 6.951   -34.421 12.407  1.00 23.86 ? 244 GLN A OE1 1 
ATOM   1927 N NE2 . GLN A 1 243 ? 5.382   -33.825 13.909  1.00 29.89 ? 244 GLN A NE2 1 
ATOM   1928 N N   . LYS A 1 244 ? 3.937   -33.819 9.548   1.00 25.42 ? 245 LYS A N   1 
ATOM   1929 C CA  . LYS A 1 244 ? 2.673   -33.171 9.232   1.00 23.90 ? 245 LYS A CA  1 
ATOM   1930 C C   . LYS A 1 244 ? 2.475   -32.945 7.736   1.00 27.20 ? 245 LYS A C   1 
ATOM   1931 O O   . LYS A 1 244 ? 1.389   -32.517 7.330   1.00 28.17 ? 245 LYS A O   1 
ATOM   1932 C CB  . LYS A 1 244 ? 2.570   -31.841 9.985   1.00 26.00 ? 245 LYS A CB  1 
ATOM   1933 C CG  . LYS A 1 244 ? 2.370   -32.038 11.483  1.00 32.05 ? 245 LYS A CG  1 
ATOM   1934 C CD  . LYS A 1 244 ? 2.425   -30.742 12.264  1.00 39.23 ? 245 LYS A CD  1 
ATOM   1935 C CE  . LYS A 1 244 ? 2.035   -31.006 13.713  1.00 44.11 ? 245 LYS A CE  1 
ATOM   1936 N NZ  . LYS A 1 244 ? 0.857   -31.935 13.752  1.00 53.96 ? 245 LYS A NZ  1 
ATOM   1937 N N   . TYR A 1 245 ? 3.479   -33.238 6.915   1.00 23.57 ? 246 TYR A N   1 
ATOM   1938 C CA  . TYR A 1 245 ? 3.482   -33.021 5.472   1.00 23.38 ? 246 TYR A CA  1 
ATOM   1939 C C   . TYR A 1 245 ? 3.260   -34.331 4.729   1.00 23.23 ? 246 TYR A C   1 
ATOM   1940 O O   . TYR A 1 245 ? 3.528   -35.415 5.260   1.00 23.26 ? 246 TYR A O   1 
ATOM   1941 C CB  . TYR A 1 245 ? 4.817   -32.379 5.041   1.00 21.24 ? 246 TYR A CB  1 
ATOM   1942 C CG  . TYR A 1 245 ? 4.919   -30.943 5.482   1.00 20.67 ? 246 TYR A CG  1 
ATOM   1943 C CD1 . TYR A 1 245 ? 5.078   -30.615 6.827   1.00 22.53 ? 246 TYR A CD1 1 
ATOM   1944 C CD2 . TYR A 1 245 ? 4.822   -29.909 4.561   1.00 20.69 ? 246 TYR A CD2 1 
ATOM   1945 C CE1 . TYR A 1 245 ? 5.135   -29.282 7.240   1.00 22.51 ? 246 TYR A CE1 1 
ATOM   1946 C CE2 . TYR A 1 245 ? 4.893   -28.597 4.958   1.00 21.86 ? 246 TYR A CE2 1 
ATOM   1947 C CZ  . TYR A 1 245 ? 5.053   -28.286 6.296   1.00 21.49 ? 246 TYR A CZ  1 
ATOM   1948 O OH  . TYR A 1 245 ? 5.099   -26.962 6.673   1.00 23.90 ? 246 TYR A OH  1 
ATOM   1949 N N   . PRO A 1 246 ? 2.748   -34.272 3.495   1.00 23.34 ? 247 PRO A N   1 
ATOM   1950 C CA  . PRO A 1 246 ? 2.517   -35.502 2.726   1.00 24.41 ? 247 PRO A CA  1 
ATOM   1951 C C   . PRO A 1 246 ? 3.814   -36.258 2.473   1.00 21.45 ? 247 PRO A C   1 
ATOM   1952 O O   . PRO A 1 246 ? 4.912   -35.696 2.498   1.00 22.31 ? 247 PRO A O   1 
ATOM   1953 C CB  . PRO A 1 246 ? 1.894   -34.993 1.412   1.00 24.72 ? 247 PRO A CB  1 
ATOM   1954 C CG  . PRO A 1 246 ? 1.331   -33.647 1.765   1.00 24.36 ? 247 PRO A CG  1 
ATOM   1955 C CD  . PRO A 1 246 ? 2.265   -33.074 2.787   1.00 23.09 ? 247 PRO A CD  1 
ATOM   1956 N N   . ALA A 1 247 ? 3.662   -37.558 2.197   1.00 21.92 ? 248 ALA A N   1 
ATOM   1957 C CA  . ALA A 1 247 ? 4.784   -38.490 2.288   1.00 22.29 ? 248 ALA A CA  1 
ATOM   1958 C C   . ALA A 1 247 ? 5.951   -38.099 1.387   1.00 22.92 ? 248 ALA A C   1 
ATOM   1959 O O   . ALA A 1 247 ? 7.107   -38.167 1.813   1.00 21.46 ? 248 ALA A O   1 
ATOM   1960 C CB  . ALA A 1 247 ? 4.316   -39.908 1.960   1.00 23.91 ? 248 ALA A CB  1 
ATOM   1961 N N   . ASP A 1 248 ? 5.688   -37.702 0.136   1.00 21.55 ? 249 ASP A N   1 
ATOM   1962 C CA  . ASP A 1 248 ? 6.810   -37.460 -0.773  1.00 23.60 ? 249 ASP A CA  1 
ATOM   1963 C C   . ASP A 1 248 ? 7.721   -36.334 -0.274  1.00 23.27 ? 249 ASP A C   1 
ATOM   1964 O O   . ASP A 1 248 ? 8.958   -36.447 -0.344  1.00 21.40 ? 249 ASP A O   1 
ATOM   1965 C CB  . ASP A 1 248 ? 6.298   -37.183 -2.192  1.00 25.88 ? 249 ASP A CB  1 
ATOM   1966 C CG  . ASP A 1 248 ? 5.716   -38.448 -2.883  1.00 29.29 ? 249 ASP A CG  1 
ATOM   1967 O OD1 . ASP A 1 248 ? 6.011   -39.599 -2.469  1.00 27.53 ? 249 ASP A OD1 1 
ATOM   1968 O OD2 . ASP A 1 248 ? 4.949   -38.295 -3.860  1.00 33.23 ? 249 ASP A OD2 1 
ATOM   1969 N N   . ILE A 1 249 ? 7.148   -35.240 0.242   1.00 22.94 ? 250 ILE A N   1 
ATOM   1970 C CA  . ILE A 1 249 ? 8.009   -34.175 0.746   1.00 19.96 ? 250 ILE A CA  1 
ATOM   1971 C C   . ILE A 1 249 ? 8.479   -34.487 2.174   1.00 20.23 ? 250 ILE A C   1 
ATOM   1972 O O   . ILE A 1 249 ? 9.599   -34.110 2.552   1.00 18.02 ? 250 ILE A O   1 
ATOM   1973 C CB  . ILE A 1 249 ? 7.315   -32.795 0.638   1.00 21.55 ? 250 ILE A CB  1 
ATOM   1974 C CG1 . ILE A 1 249 ? 8.314   -31.649 0.834   1.00 22.09 ? 250 ILE A CG1 1 
ATOM   1975 C CG2 . ILE A 1 249 ? 6.144   -32.659 1.629   1.00 20.56 ? 250 ILE A CG2 1 
ATOM   1976 C CD1 . ILE A 1 249 ? 9.433   -31.564 -0.221  1.00 19.13 ? 250 ILE A CD1 1 
ATOM   1977 N N   . GLN A 1 250 ? 7.662   -35.190 2.972   1.00 20.26 ? 251 GLN A N   1 
ATOM   1978 C CA  A GLN A 1 250 ? 8.111   -35.622 4.298   0.56 21.00 ? 251 GLN A CA  1 
ATOM   1979 C CA  B GLN A 1 250 ? 8.101   -35.638 4.296   0.44 20.75 ? 251 GLN A CA  1 
ATOM   1980 C C   . GLN A 1 250 ? 9.369   -36.476 4.198   1.00 19.71 ? 251 GLN A C   1 
ATOM   1981 O O   . GLN A 1 250 ? 10.336  -36.264 4.943   1.00 19.89 ? 251 GLN A O   1 
ATOM   1982 C CB  A GLN A 1 250 ? 7.003   -36.387 5.032   0.56 19.73 ? 251 GLN A CB  1 
ATOM   1983 C CB  B GLN A 1 250 ? 6.990   -36.440 4.974   0.44 19.43 ? 251 GLN A CB  1 
ATOM   1984 C CG  A GLN A 1 250 ? 7.468   -36.979 6.374   0.56 22.41 ? 251 GLN A CG  1 
ATOM   1985 C CG  B GLN A 1 250 ? 7.464   -37.305 6.141   0.44 22.42 ? 251 GLN A CG  1 
ATOM   1986 C CD  A GLN A 1 250 ? 6.355   -37.618 7.205   0.56 23.48 ? 251 GLN A CD  1 
ATOM   1987 C CD  B GLN A 1 250 ? 6.763   -38.653 6.201   0.44 22.70 ? 251 GLN A CD  1 
ATOM   1988 O OE1 A GLN A 1 250 ? 6.622   -38.255 8.233   0.56 22.31 ? 251 GLN A OE1 1 
ATOM   1989 O OE1 B GLN A 1 250 ? 6.895   -39.477 5.298   0.44 21.63 ? 251 GLN A OE1 1 
ATOM   1990 N NE2 A GLN A 1 250 ? 5.106   -37.439 6.778   0.56 22.85 ? 251 GLN A NE2 1 
ATOM   1991 N NE2 B GLN A 1 250 ? 6.004   -38.876 7.265   0.44 25.11 ? 251 GLN A NE2 1 
ATOM   1992 N N   . ARG A 1 251 ? 9.379   -37.445 3.280   1.00 18.98 ? 252 ARG A N   1 
ATOM   1993 C CA  . ARG A 1 251 ? 10.552  -38.294 3.111   1.00 19.51 ? 252 ARG A CA  1 
ATOM   1994 C C   . ARG A 1 251 ? 11.747  -37.498 2.625   1.00 18.32 ? 252 ARG A C   1 
ATOM   1995 O O   . ARG A 1 251 ? 12.880  -37.731 3.068   1.00 20.31 ? 252 ARG A O   1 
ATOM   1996 C CB  . ARG A 1 251 ? 10.227  -39.433 2.141   1.00 21.68 ? 252 ARG A CB  1 
ATOM   1997 C CG  . ARG A 1 251 ? 9.268   -40.459 2.764   1.00 26.26 ? 252 ARG A CG  1 
ATOM   1998 C CD  . ARG A 1 251 ? 8.441   -41.232 1.734   1.00 25.98 ? 252 ARG A CD  1 
ATOM   1999 N NE  . ARG A 1 251 ? 9.228   -41.884 0.692   1.00 29.23 ? 252 ARG A NE  1 
ATOM   2000 C CZ  . ARG A 1 251 ? 9.651   -43.145 0.738   1.00 30.93 ? 252 ARG A CZ  1 
ATOM   2001 N NH1 . ARG A 1 251 ? 9.500   -43.891 1.823   1.00 29.54 ? 252 ARG A NH1 1 
ATOM   2002 N NH2 . ARG A 1 251 ? 10.236  -43.675 -0.335  1.00 28.47 ? 252 ARG A NH2 1 
ATOM   2003 N N   . ALA A 1 252 ? 11.515  -36.540 1.723   1.00 18.64 ? 253 ALA A N   1 
ATOM   2004 C CA  . ALA A 1 252 ? 12.590  -35.663 1.269   1.00 17.95 ? 253 ALA A CA  1 
ATOM   2005 C C   . ALA A 1 252 ? 13.225  -34.907 2.436   1.00 20.73 ? 253 ALA A C   1 
ATOM   2006 O O   . ALA A 1 252 ? 14.458  -34.832 2.550   1.00 18.28 ? 253 ALA A O   1 
ATOM   2007 C CB  . ALA A 1 252 ? 12.053  -34.672 0.234   1.00 16.55 ? 253 ALA A CB  1 
ATOM   2008 N N   . ILE A 1 253 ? 12.392  -34.324 3.304   1.00 18.42 ? 254 ILE A N   1 
ATOM   2009 C CA  . ILE A 1 253 ? 12.906  -33.497 4.393   1.00 17.99 ? 254 ILE A CA  1 
ATOM   2010 C C   . ILE A 1 253 ? 13.719  -34.343 5.368   1.00 20.32 ? 254 ILE A C   1 
ATOM   2011 O O   . ILE A 1 253 ? 14.819  -33.954 5.792   1.00 19.37 ? 254 ILE A O   1 
ATOM   2012 C CB  . ILE A 1 253 ? 11.753  -32.772 5.112   1.00 21.45 ? 254 ILE A CB  1 
ATOM   2013 C CG1 . ILE A 1 253 ? 11.118  -31.688 4.218   1.00 19.73 ? 254 ILE A CG1 1 
ATOM   2014 C CG2 . ILE A 1 253 ? 12.257  -32.155 6.434   1.00 19.87 ? 254 ILE A CG2 1 
ATOM   2015 C CD1 . ILE A 1 253 ? 9.733   -31.297 4.689   1.00 21.40 ? 254 ILE A CD1 1 
ATOM   2016 N N   . ASN A 1 254 ? 13.193  -35.514 5.734   1.00 19.74 ? 255 ASN A N   1 
ATOM   2017 C CA  . ASN A 1 254 ? 13.915  -36.397 6.648   1.00 20.93 ? 255 ASN A CA  1 
ATOM   2018 C C   . ASN A 1 254 ? 15.257  -36.825 6.062   1.00 21.04 ? 255 ASN A C   1 
ATOM   2019 O O   . ASN A 1 254 ? 16.257  -36.942 6.790   1.00 19.77 ? 255 ASN A O   1 
ATOM   2020 C CB  . ASN A 1 254 ? 13.033  -37.602 6.997   1.00 19.57 ? 255 ASN A CB  1 
ATOM   2021 C CG  . ASN A 1 254 ? 12.004  -37.259 8.053   1.00 24.56 ? 255 ASN A CG  1 
ATOM   2022 O OD1 . ASN A 1 254 ? 12.319  -36.579 9.031   1.00 25.98 ? 255 ASN A OD1 1 
ATOM   2023 N ND2 . ASN A 1 254 ? 10.768  -37.701 7.858   1.00 22.48 ? 255 ASN A ND2 1 
ATOM   2024 N N   . GLU A 1 255 ? 15.307  -37.025 4.741   1.00 19.36 ? 256 GLU A N   1 
ATOM   2025 C CA  . GLU A 1 255 ? 16.568  -37.349 4.077   1.00 19.95 ? 256 GLU A CA  1 
ATOM   2026 C C   . GLU A 1 255 ? 17.625  -36.267 4.294   1.00 19.81 ? 256 GLU A C   1 
ATOM   2027 O O   . GLU A 1 255 ? 18.827  -36.570 4.342   1.00 19.02 ? 256 GLU A O   1 
ATOM   2028 C CB  . GLU A 1 255 ? 16.315  -37.563 2.580   1.00 20.01 ? 256 GLU A CB  1 
ATOM   2029 C CG  . GLU A 1 255 ? 17.373  -38.388 1.847   1.00 21.83 ? 256 GLU A CG  1 
ATOM   2030 C CD  . GLU A 1 255 ? 17.374  -39.874 2.261   1.00 23.31 ? 256 GLU A CD  1 
ATOM   2031 O OE1 . GLU A 1 255 ? 16.314  -40.533 2.253   1.00 26.10 ? 256 GLU A OE1 1 
ATOM   2032 O OE2 . GLU A 1 255 ? 18.454  -40.369 2.605   1.00 26.81 ? 256 GLU A OE2 1 
ATOM   2033 N N   . THR A 1 256 ? 17.218  -35.000 4.411   1.00 19.95 ? 257 THR A N   1 
ATOM   2034 C CA  . THR A 1 256 ? 18.221  -33.967 4.630   1.00 18.13 ? 257 THR A CA  1 
ATOM   2035 C C   . THR A 1 256 ? 18.686  -33.904 6.077   1.00 19.97 ? 257 THR A C   1 
ATOM   2036 O O   . THR A 1 256 ? 19.581  -33.114 6.376   1.00 23.07 ? 257 THR A O   1 
ATOM   2037 C CB  . THR A 1 256 ? 17.710  -32.577 4.204   1.00 18.16 ? 257 THR A CB  1 
ATOM   2038 O OG1 . THR A 1 256 ? 16.731  -32.076 5.140   1.00 17.28 ? 257 THR A OG1 1 
ATOM   2039 C CG2 . THR A 1 256 ? 17.120  -32.630 2.808   1.00 18.24 ? 257 THR A CG2 1 
ATOM   2040 N N   . HIS A 1 257 ? 18.107  -34.695 6.976   1.00 16.70 ? 258 HIS A N   1 
ATOM   2041 C CA  . HIS A 1 257 ? 18.470  -34.638 8.387   1.00 18.78 ? 258 HIS A CA  1 
ATOM   2042 C C   . HIS A 1 257 ? 19.457  -35.719 8.813   1.00 21.62 ? 258 HIS A C   1 
ATOM   2043 O O   . HIS A 1 257 ? 19.995  -35.633 9.919   1.00 22.46 ? 258 HIS A O   1 
ATOM   2044 C CB  . HIS A 1 257 ? 17.216  -34.723 9.269   1.00 19.78 ? 258 HIS A CB  1 
ATOM   2045 C CG  . HIS A 1 257 ? 16.311  -33.528 9.155   1.00 19.49 ? 258 HIS A CG  1 
ATOM   2046 N ND1 . HIS A 1 257 ? 15.101  -33.446 9.811   1.00 19.63 ? 258 HIS A ND1 1 
ATOM   2047 C CD2 . HIS A 1 257 ? 16.430  -32.382 8.441   1.00 17.77 ? 258 HIS A CD2 1 
ATOM   2048 C CE1 . HIS A 1 257 ? 14.526  -32.289 9.524   1.00 20.35 ? 258 HIS A CE1 1 
ATOM   2049 N NE2 . HIS A 1 257 ? 15.303  -31.633 8.682   1.00 19.40 ? 258 HIS A NE2 1 
ATOM   2050 N N   . GLN A 1 258 ? 19.712  -36.720 7.975   1.00 22.15 ? 259 GLN A N   1 
ATOM   2051 C CA  . GLN A 1 258 ? 20.567  -37.837 8.351   1.00 22.32 ? 259 GLN A CA  1 
ATOM   2052 C C   . GLN A 1 258 ? 22.036  -37.427 8.241   1.00 19.61 ? 259 GLN A C   1 
ATOM   2053 O O   . GLN A 1 258 ? 22.491  -37.009 7.174   1.00 19.02 ? 259 GLN A O   1 
ATOM   2054 C CB  . GLN A 1 258 ? 20.267  -39.039 7.450   1.00 24.15 ? 259 GLN A CB  1 
ATOM   2055 C CG  . GLN A 1 258 ? 21.000  -40.294 7.850   1.00 30.36 ? 259 GLN A CG  1 
ATOM   2056 C CD  . GLN A 1 258 ? 20.876  -41.411 6.819   1.00 36.09 ? 259 GLN A CD  1 
ATOM   2057 O OE1 . GLN A 1 258 ? 19.865  -41.522 6.114   1.00 38.03 ? 259 GLN A OE1 1 
ATOM   2058 N NE2 . GLN A 1 258 ? 21.912  -42.246 6.729   1.00 35.63 ? 259 GLN A NE2 1 
ATOM   2059 N N   . GLY A 1 259 ? 22.777  -37.538 9.333   1.00 23.56 ? 260 GLY A N   1 
ATOM   2060 C CA  . GLY A 1 259 ? 24.216  -37.321 9.255   1.00 23.22 ? 260 GLY A CA  1 
ATOM   2061 C C   . GLY A 1 259 ? 24.914  -38.309 8.332   1.00 22.29 ? 260 GLY A C   1 
ATOM   2062 O O   . GLY A 1 259 ? 24.672  -39.518 8.418   1.00 21.18 ? 260 GLY A O   1 
ATOM   2063 N N   . ARG A 1 260 ? 25.798  -37.816 7.463   1.00 19.61 ? 261 ARG A N   1 
ATOM   2064 C CA  . ARG A 1 260 ? 26.493  -38.663 6.501   1.00 18.66 ? 261 ARG A CA  1 
ATOM   2065 C C   . ARG A 1 260 ? 27.933  -38.985 6.895   1.00 22.42 ? 261 ARG A C   1 
ATOM   2066 O O   . ARG A 1 260 ? 28.432  -40.066 6.555   1.00 22.57 ? 261 ARG A O   1 
ATOM   2067 C CB  . ARG A 1 260 ? 26.472  -38.004 5.115   1.00 17.36 ? 261 ARG A CB  1 
ATOM   2068 C CG  . ARG A 1 260 ? 25.036  -37.706 4.602   1.00 20.13 ? 261 ARG A CG  1 
ATOM   2069 C CD  . ARG A 1 260 ? 24.148  -38.952 4.509   1.00 22.20 ? 261 ARG A CD  1 
ATOM   2070 N NE  . ARG A 1 260 ? 22.768  -38.597 4.168   1.00 22.86 ? 261 ARG A NE  1 
ATOM   2071 C CZ  . ARG A 1 260 ? 21.876  -39.415 3.625   1.00 23.53 ? 261 ARG A CZ  1 
ATOM   2072 N NH1 . ARG A 1 260 ? 22.185  -40.659 3.285   1.00 23.19 ? 261 ARG A NH1 1 
ATOM   2073 N NH2 . ARG A 1 260 ? 20.645  -38.972 3.406   1.00 22.61 ? 261 ARG A NH2 1 
ATOM   2074 N N   . TYR A 1 261 ? 28.604  -38.081 7.596   1.00 18.54 ? 262 TYR A N   1 
ATOM   2075 C CA  . TYR A 1 261 ? 29.943  -38.296 8.143   1.00 19.29 ? 262 TYR A CA  1 
ATOM   2076 C C   . TYR A 1 261 ? 30.163  -37.209 9.184   1.00 19.53 ? 262 TYR A C   1 
ATOM   2077 O O   . TYR A 1 261 ? 29.322  -36.326 9.368   1.00 19.10 ? 262 TYR A O   1 
ATOM   2078 C CB  . TYR A 1 261 ? 31.036  -38.258 7.060   1.00 19.59 ? 262 TYR A CB  1 
ATOM   2079 C CG  . TYR A 1 261 ? 31.086  -36.965 6.257   1.00 19.34 ? 262 TYR A CG  1 
ATOM   2080 C CD1 . TYR A 1 261 ? 31.640  -35.804 6.794   1.00 19.67 ? 262 TYR A CD1 1 
ATOM   2081 C CD2 . TYR A 1 261 ? 30.585  -36.906 4.957   1.00 18.90 ? 262 TYR A CD2 1 
ATOM   2082 C CE1 . TYR A 1 261 ? 31.677  -34.615 6.072   1.00 19.54 ? 262 TYR A CE1 1 
ATOM   2083 C CE2 . TYR A 1 261 ? 30.634  -35.717 4.213   1.00 18.78 ? 262 TYR A CE2 1 
ATOM   2084 C CZ  . TYR A 1 261 ? 31.178  -34.575 4.786   1.00 19.09 ? 262 TYR A CZ  1 
ATOM   2085 O OH  . TYR A 1 261 ? 31.233  -33.395 4.063   1.00 19.09 ? 262 TYR A OH  1 
ATOM   2086 N N   . GLN A 1 262 ? 31.322  -37.251 9.833   1.00 20.33 ? 263 GLN A N   1 
ATOM   2087 C CA  . GLN A 1 262 ? 31.636  -36.366 10.940  1.00 20.82 ? 263 GLN A CA  1 
ATOM   2088 C C   . GLN A 1 262 ? 32.960  -35.672 10.666  1.00 21.50 ? 263 GLN A C   1 
ATOM   2089 O O   . GLN A 1 262 ? 33.900  -36.287 10.154  1.00 21.95 ? 263 GLN A O   1 
ATOM   2090 C CB  . GLN A 1 262 ? 31.711  -37.155 12.268  1.00 23.34 ? 263 GLN A CB  1 
ATOM   2091 C CG  . GLN A 1 262 ? 31.966  -36.313 13.501  1.00 26.56 ? 263 GLN A CG  1 
ATOM   2092 C CD  . GLN A 1 262 ? 31.794  -37.113 14.786  1.00 30.58 ? 263 GLN A CD  1 
ATOM   2093 O OE1 . GLN A 1 262 ? 31.674  -38.336 14.759  1.00 29.76 ? 263 GLN A OE1 1 
ATOM   2094 N NE2 . GLN A 1 262 ? 31.772  -36.422 15.913  1.00 36.19 ? 263 GLN A NE2 1 
ATOM   2095 N N   . VAL A 1 263 ? 33.027  -34.385 10.994  1.00 21.68 ? 264 VAL A N   1 
ATOM   2096 C CA  . VAL A 1 263 ? 34.283  -33.645 11.004  1.00 22.58 ? 264 VAL A CA  1 
ATOM   2097 C C   . VAL A 1 263 ? 34.336  -32.954 12.358  1.00 25.33 ? 264 VAL A C   1 
ATOM   2098 O O   . VAL A 1 263 ? 33.662  -31.942 12.565  1.00 24.85 ? 264 VAL A O   1 
ATOM   2099 C CB  . VAL A 1 263 ? 34.393  -32.629 9.861   1.00 29.38 ? 264 VAL A CB  1 
ATOM   2100 C CG1 . VAL A 1 263 ? 35.702  -31.859 9.978   1.00 29.79 ? 264 VAL A CG1 1 
ATOM   2101 C CG2 . VAL A 1 263 ? 34.348  -33.332 8.531   1.00 27.40 ? 264 VAL A CG2 1 
ATOM   2102 N N   . ASN A 1 264 ? 35.119  -33.505 13.287  1.00 29.16 ? 265 ASN A N   1 
ATOM   2103 C CA  . ASN A 1 264 ? 35.250  -32.967 14.647  1.00 28.55 ? 265 ASN A CA  1 
ATOM   2104 C C   . ASN A 1 264 ? 33.864  -32.938 15.276  1.00 27.07 ? 265 ASN A C   1 
ATOM   2105 O O   . ASN A 1 264 ? 33.217  -33.996 15.355  1.00 29.39 ? 265 ASN A O   1 
ATOM   2106 C CB  . ASN A 1 264 ? 35.962  -31.617 14.595  1.00 30.51 ? 265 ASN A CB  1 
ATOM   2107 C CG  . ASN A 1 264 ? 37.269  -31.684 13.851  1.00 38.76 ? 265 ASN A CG  1 
ATOM   2108 O OD1 . ASN A 1 264 ? 37.586  -30.806 13.045  1.00 41.85 ? 265 ASN A OD1 1 
ATOM   2109 N ND2 . ASN A 1 264 ? 38.035  -32.729 14.109  1.00 37.43 ? 265 ASN A ND2 1 
ATOM   2110 N N   . THR A 1 265 ? 33.362  -31.789 15.708  1.00 25.81 ? 266 THR A N   1 
ATOM   2111 C CA  . THR A 1 265 ? 32.073  -31.721 16.370  1.00 26.92 ? 266 THR A CA  1 
ATOM   2112 C C   . THR A 1 265 ? 30.911  -31.497 15.409  1.00 23.24 ? 266 THR A C   1 
ATOM   2113 O O   . THR A 1 265 ? 29.763  -31.400 15.861  1.00 25.13 ? 266 THR A O   1 
ATOM   2114 C CB  . THR A 1 265 ? 32.096  -30.607 17.412  1.00 26.83 ? 266 THR A CB  1 
ATOM   2115 O OG1 . THR A 1 265 ? 32.628  -29.417 16.811  1.00 30.04 ? 266 THR A OG1 1 
ATOM   2116 C CG2 . THR A 1 265 ? 32.947  -31.013 18.588  1.00 29.74 ? 266 THR A CG2 1 
ATOM   2117 N N   . MET A 1 266 ? 31.169  -31.404 14.110  1.00 24.36 ? 267 MET A N   1 
ATOM   2118 C CA  A MET A 1 266 ? 30.126  -31.181 13.118  0.45 22.54 ? 267 MET A CA  1 
ATOM   2119 C CA  B MET A 1 266 ? 30.118  -31.184 13.121  0.55 22.47 ? 267 MET A CA  1 
ATOM   2120 C C   . MET A 1 266 ? 29.806  -32.475 12.373  1.00 22.97 ? 267 MET A C   1 
ATOM   2121 O O   . MET A 1 266 ? 30.704  -33.256 12.051  1.00 23.67 ? 267 MET A O   1 
ATOM   2122 C CB  A MET A 1 266 ? 30.568  -30.099 12.133  0.45 22.63 ? 267 MET A CB  1 
ATOM   2123 C CB  B MET A 1 266 ? 30.519  -30.092 12.121  0.55 22.63 ? 267 MET A CB  1 
ATOM   2124 C CG  A MET A 1 266 ? 29.514  -29.691 11.131  0.45 25.20 ? 267 MET A CG  1 
ATOM   2125 C CG  B MET A 1 266 ? 29.387  -29.636 11.179  0.55 25.18 ? 267 MET A CG  1 
ATOM   2126 S SD  A MET A 1 266 ? 30.128  -28.375 10.067  0.45 32.50 ? 267 MET A SD  1 
ATOM   2127 S SD  B MET A 1 266 ? 29.280  -30.512 9.591   0.55 23.87 ? 267 MET A SD  1 
ATOM   2128 C CE  A MET A 1 266 ? 31.486  -29.182 9.221   0.45 25.94 ? 267 MET A CE  1 
ATOM   2129 C CE  B MET A 1 266 ? 30.969  -30.385 9.016   0.55 24.66 ? 267 MET A CE  1 
ATOM   2130 N N   . TYR A 1 267 ? 28.523  -32.701 12.100  1.00 19.61 ? 268 TYR A N   1 
ATOM   2131 C CA  . TYR A 1 267 ? 28.089  -33.825 11.276  1.00 19.13 ? 268 TYR A CA  1 
ATOM   2132 C C   . TYR A 1 267 ? 27.492  -33.237 10.009  1.00 21.06 ? 268 TYR A C   1 
ATOM   2133 O O   . TYR A 1 267 ? 26.641  -32.348 10.091  1.00 21.98 ? 268 TYR A O   1 
ATOM   2134 C CB  . TYR A 1 267 ? 27.043  -34.693 11.981  1.00 22.13 ? 268 TYR A CB  1 
ATOM   2135 C CG  . TYR A 1 267 ? 27.490  -35.288 13.300  1.00 24.26 ? 268 TYR A CG  1 
ATOM   2136 C CD1 . TYR A 1 267 ? 27.491  -34.522 14.464  1.00 26.95 ? 268 TYR A CD1 1 
ATOM   2137 C CD2 . TYR A 1 267 ? 27.897  -36.609 13.387  1.00 27.55 ? 268 TYR A CD2 1 
ATOM   2138 C CE1 . TYR A 1 267 ? 27.893  -35.058 15.685  1.00 27.41 ? 268 TYR A CE1 1 
ATOM   2139 C CE2 . TYR A 1 267 ? 28.294  -37.156 14.606  1.00 29.98 ? 268 TYR A CE2 1 
ATOM   2140 C CZ  . TYR A 1 267 ? 28.291  -36.372 15.750  1.00 31.29 ? 268 TYR A CZ  1 
ATOM   2141 O OH  . TYR A 1 267 ? 28.692  -36.908 16.957  1.00 31.38 ? 268 TYR A OH  1 
ATOM   2142 N N   . GLN A 1 268 ? 27.979  -33.674 8.847   1.00 18.24 ? 269 GLN A N   1 
ATOM   2143 C CA  . GLN A 1 268 ? 27.474  -33.164 7.576   1.00 17.72 ? 269 GLN A CA  1 
ATOM   2144 C C   . GLN A 1 268 ? 26.257  -33.974 7.147   1.00 19.23 ? 269 GLN A C   1 
ATOM   2145 O O   . GLN A 1 268 ? 26.363  -35.190 6.910   1.00 19.20 ? 269 GLN A O   1 
ATOM   2146 C CB  . GLN A 1 268 ? 28.542  -33.231 6.489   1.00 17.99 ? 269 GLN A CB  1 
ATOM   2147 C CG  . GLN A 1 268 ? 28.067  -32.665 5.137   1.00 17.60 ? 269 GLN A CG  1 
ATOM   2148 C CD  . GLN A 1 268 ? 27.934  -31.148 5.167   1.00 20.74 ? 269 GLN A CD  1 
ATOM   2149 O OE1 . GLN A 1 268 ? 28.908  -30.433 5.397   1.00 20.27 ? 269 GLN A OE1 1 
ATOM   2150 N NE2 . GLN A 1 268 ? 26.710  -30.654 4.982   1.00 19.10 ? 269 GLN A NE2 1 
ATOM   2151 N N   . ALA A 1 269 ? 25.114  -33.308 7.034   1.00 20.45 ? 270 ALA A N   1 
ATOM   2152 C CA  . ALA A 1 269 ? 23.933  -33.889 6.414   1.00 20.05 ? 270 ALA A CA  1 
ATOM   2153 C C   . ALA A 1 269 ? 23.808  -33.367 4.978   1.00 20.20 ? 270 ALA A C   1 
ATOM   2154 O O   . ALA A 1 269 ? 24.710  -32.721 4.450   1.00 20.17 ? 270 ALA A O   1 
ATOM   2155 C CB  . ALA A 1 269 ? 22.694  -33.577 7.256   1.00 19.65 ? 270 ALA A CB  1 
ATOM   2156 N N   . LEU A 1 270 ? 22.691  -33.662 4.313   1.00 21.54 ? 271 LEU A N   1 
ATOM   2157 C CA  . LEU A 1 270 ? 22.440  -33.049 3.006   1.00 20.07 ? 271 LEU A CA  1 
ATOM   2158 C C   . LEU A 1 270 ? 22.057  -31.591 3.208   1.00 19.33 ? 271 LEU A C   1 
ATOM   2159 O O   . LEU A 1 270 ? 20.974  -31.303 3.716   1.00 22.63 ? 271 LEU A O   1 
ATOM   2160 C CB  . LEU A 1 270 ? 21.324  -33.774 2.256   1.00 22.99 ? 271 LEU A CB  1 
ATOM   2161 C CG  . LEU A 1 270 ? 21.594  -35.194 1.799   1.00 25.49 ? 271 LEU A CG  1 
ATOM   2162 C CD1 . LEU A 1 270 ? 20.354  -35.716 1.062   1.00 24.36 ? 271 LEU A CD1 1 
ATOM   2163 C CD2 . LEU A 1 270 ? 22.794  -35.198 0.881   1.00 25.45 ? 271 LEU A CD2 1 
ATOM   2164 N N   . GLY A 1 271 ? 22.923  -30.680 2.788   1.00 17.69 ? 272 GLY A N   1 
ATOM   2165 C CA  . GLY A 1 271 ? 22.714  -29.264 2.992   1.00 19.03 ? 272 GLY A CA  1 
ATOM   2166 C C   . GLY A 1 271 ? 22.972  -28.799 4.413   1.00 19.14 ? 272 GLY A C   1 
ATOM   2167 O O   . GLY A 1 271 ? 23.881  -27.993 4.643   1.00 20.34 ? 272 GLY A O   1 
ATOM   2168 N N   . TRP A 1 272 ? 22.166  -29.286 5.359   1.00 18.63 ? 273 TRP A N   1 
ATOM   2169 C CA  . TRP A 1 272 ? 22.298  -28.918 6.767   1.00 17.68 ? 273 TRP A CA  1 
ATOM   2170 C C   . TRP A 1 272 ? 23.625  -29.382 7.368   1.00 17.21 ? 273 TRP A C   1 
ATOM   2171 O O   . TRP A 1 272 ? 24.110  -30.487 7.092   1.00 17.99 ? 273 TRP A O   1 
ATOM   2172 C CB  . TRP A 1 272 ? 21.155  -29.527 7.584   1.00 15.97 ? 273 TRP A CB  1 
ATOM   2173 C CG  . TRP A 1 272 ? 19.769  -29.019 7.250   1.00 21.66 ? 273 TRP A CG  1 
ATOM   2174 C CD1 . TRP A 1 272 ? 18.809  -29.667 6.512   1.00 20.94 ? 273 TRP A CD1 1 
ATOM   2175 C CD2 . TRP A 1 272 ? 19.190  -27.773 7.656   1.00 19.08 ? 273 TRP A CD2 1 
ATOM   2176 N NE1 . TRP A 1 272 ? 17.676  -28.887 6.426   1.00 22.77 ? 273 TRP A NE1 1 
ATOM   2177 C CE2 . TRP A 1 272 ? 17.874  -27.726 7.124   1.00 17.60 ? 273 TRP A CE2 1 
ATOM   2178 C CE3 . TRP A 1 272 ? 19.648  -26.694 8.415   1.00 17.15 ? 273 TRP A CE3 1 
ATOM   2179 C CZ2 . TRP A 1 272 ? 17.014  -26.644 7.333   1.00 19.89 ? 273 TRP A CZ2 1 
ATOM   2180 C CZ3 . TRP A 1 272 ? 18.795  -25.617 8.628   1.00 16.32 ? 273 TRP A CZ3 1 
ATOM   2181 C CH2 . TRP A 1 272 ? 17.482  -25.601 8.086   1.00 17.91 ? 273 TRP A CH2 1 
ATOM   2182 N N   . GLU A 1 273 ? 24.187  -28.531 8.230   1.00 18.62 ? 274 GLU A N   1 
ATOM   2183 C CA  . GLU A 1 273 ? 25.209  -28.929 9.191   1.00 21.37 ? 274 GLU A CA  1 
ATOM   2184 C C   . GLU A 1 273 ? 24.514  -29.292 10.495  1.00 24.09 ? 274 GLU A C   1 
ATOM   2185 O O   . GLU A 1 273 ? 23.530  -28.652 10.877  1.00 25.37 ? 274 GLU A O   1 
ATOM   2186 C CB  . GLU A 1 273 ? 26.210  -27.800 9.428   1.00 23.16 ? 274 GLU A CB  1 
ATOM   2187 C CG  . GLU A 1 273 ? 26.939  -27.392 8.185   1.00 29.64 ? 274 GLU A CG  1 
ATOM   2188 C CD  . GLU A 1 273 ? 27.989  -26.308 8.442   1.00 34.00 ? 274 GLU A CD  1 
ATOM   2189 O OE1 . GLU A 1 273 ? 28.006  -25.674 9.534   1.00 36.84 ? 274 GLU A OE1 1 
ATOM   2190 O OE2 . GLU A 1 273 ? 28.817  -26.106 7.536   1.00 35.01 ? 274 GLU A OE2 1 
ATOM   2191 N N   . GLU A 1 274 ? 25.022  -30.325 11.172  1.00 22.10 ? 275 GLU A N   1 
ATOM   2192 C CA  . GLU A 1 274 ? 24.320  -30.957 12.286  1.00 22.90 ? 275 GLU A CA  1 
ATOM   2193 C C   . GLU A 1 274 ? 25.239  -31.021 13.500  1.00 25.45 ? 275 GLU A C   1 
ATOM   2194 O O   . GLU A 1 274 ? 26.469  -31.138 13.372  1.00 20.73 ? 275 GLU A O   1 
ATOM   2195 C CB  . GLU A 1 274 ? 23.828  -32.372 11.878  1.00 25.18 ? 275 GLU A CB  1 
ATOM   2196 C CG  . GLU A 1 274 ? 23.083  -33.185 12.940  1.00 28.08 ? 275 GLU A CG  1 
ATOM   2197 C CD  . GLU A 1 274 ? 22.799  -34.609 12.468  1.00 32.57 ? 275 GLU A CD  1 
ATOM   2198 O OE1 . GLU A 1 274 ? 22.999  -34.869 11.272  1.00 31.10 ? 275 GLU A OE1 1 
ATOM   2199 O OE2 . GLU A 1 274 ? 22.398  -35.472 13.286  1.00 38.48 ? 275 GLU A OE2 1 
ATOM   2200 N N   . PHE A 1 275 ? 24.629  -30.904 14.685  1.00 21.04 ? 276 PHE A N   1 
ATOM   2201 C CA  . PHE A 1 275 ? 25.354  -30.873 15.947  1.00 22.39 ? 276 PHE A CA  1 
ATOM   2202 C C   . PHE A 1 275 ? 24.585  -31.637 17.013  1.00 21.31 ? 276 PHE A C   1 
ATOM   2203 O O   . PHE A 1 275 ? 23.355  -31.738 16.963  1.00 25.52 ? 276 PHE A O   1 
ATOM   2204 C CB  . PHE A 1 275 ? 25.576  -29.428 16.432  1.00 25.98 ? 276 PHE A CB  1 
ATOM   2205 C CG  . PHE A 1 275 ? 26.215  -28.562 15.407  1.00 27.13 ? 276 PHE A CG  1 
ATOM   2206 C CD1 . PHE A 1 275 ? 27.586  -28.494 15.317  1.00 25.76 ? 276 PHE A CD1 1 
ATOM   2207 C CD2 . PHE A 1 275 ? 25.438  -27.849 14.497  1.00 26.28 ? 276 PHE A CD2 1 
ATOM   2208 C CE1 . PHE A 1 275 ? 28.191  -27.706 14.356  1.00 30.90 ? 276 PHE A CE1 1 
ATOM   2209 C CE2 . PHE A 1 275 ? 26.039  -27.070 13.531  1.00 29.88 ? 276 PHE A CE2 1 
ATOM   2210 C CZ  . PHE A 1 275 ? 27.424  -27.006 13.463  1.00 27.52 ? 276 PHE A CZ  1 
ATOM   2211 N N   . SER A 1 276 ? 25.321  -32.190 17.972  1.00 25.18 ? 277 SER A N   1 
ATOM   2212 C CA  . SER A 1 276 ? 24.684  -32.712 19.171  1.00 24.64 ? 277 SER A CA  1 
ATOM   2213 C C   . SER A 1 276 ? 24.102  -31.557 19.985  1.00 27.65 ? 277 SER A C   1 
ATOM   2214 O O   . SER A 1 276 ? 24.788  -30.560 20.226  1.00 27.63 ? 277 SER A O   1 
ATOM   2215 C CB  . SER A 1 276 ? 25.689  -33.484 20.015  1.00 27.34 ? 277 SER A CB  1 
ATOM   2216 O OG  . SER A 1 276 ? 25.061  -33.938 21.208  1.00 28.35 ? 277 SER A OG  1 
ATOM   2217 N N   . TYR A 1 277 ? 22.831  -31.689 20.408  1.00 26.55 ? 278 TYR A N   1 
ATOM   2218 C CA  . TYR A 1 277 ? 22.212  -30.647 21.231  1.00 25.44 ? 278 TYR A CA  1 
ATOM   2219 C C   . TYR A 1 277 ? 22.363  -30.981 22.713  1.00 27.84 ? 278 TYR A C   1 
ATOM   2220 O O   . TYR A 1 277 ? 22.212  -32.145 23.106  1.00 28.90 ? 278 TYR A O   1 
ATOM   2221 C CB  . TYR A 1 277 ? 20.720  -30.489 20.898  1.00 30.08 ? 278 TYR A CB  1 
ATOM   2222 C CG  . TYR A 1 277 ? 19.981  -29.540 21.837  1.00 29.54 ? 278 TYR A CG  1 
ATOM   2223 C CD1 . TYR A 1 277 ? 20.011  -28.164 21.628  1.00 31.09 ? 278 TYR A CD1 1 
ATOM   2224 C CD2 . TYR A 1 277 ? 19.285  -30.018 22.944  1.00 34.33 ? 278 TYR A CD2 1 
ATOM   2225 C CE1 . TYR A 1 277 ? 19.363  -27.293 22.492  1.00 31.42 ? 278 TYR A CE1 1 
ATOM   2226 C CE2 . TYR A 1 277 ? 18.631  -29.146 23.819  1.00 35.66 ? 278 TYR A CE2 1 
ATOM   2227 C CZ  . TYR A 1 277 ? 18.671  -27.786 23.578  1.00 37.79 ? 278 TYR A CZ  1 
ATOM   2228 O OH  . TYR A 1 277 ? 18.024  -26.902 24.427  1.00 39.93 ? 278 TYR A OH  1 
ATOM   2229 N N   . PRO A 1 278 ? 22.671  -29.997 23.567  1.00 31.27 ? 279 PRO A N   1 
ATOM   2230 C CA  . PRO A 1 278 ? 23.008  -28.602 23.246  1.00 26.14 ? 279 PRO A CA  1 
ATOM   2231 C C   . PRO A 1 278 ? 24.420  -28.442 22.698  1.00 26.91 ? 279 PRO A C   1 
ATOM   2232 O O   . PRO A 1 278 ? 25.371  -29.082 23.140  1.00 25.93 ? 279 PRO A O   1 
ATOM   2233 C CB  . PRO A 1 278 ? 22.831  -27.873 24.595  1.00 28.17 ? 279 PRO A CB  1 
ATOM   2234 C CG  . PRO A 1 278 ? 22.918  -28.924 25.638  1.00 31.92 ? 279 PRO A CG  1 
ATOM   2235 C CD  . PRO A 1 278 ? 22.394  -30.179 25.003  1.00 30.16 ? 279 PRO A CD  1 
ATOM   2236 N N   . ALA A 1 279 ? 24.574  -27.572 21.704  1.00 27.75 ? 280 ALA A N   1 
ATOM   2237 C CA  . ALA A 1 279 ? 25.883  -27.224 21.180  1.00 26.15 ? 280 ALA A CA  1 
ATOM   2238 C C   . ALA A 1 279 ? 26.392  -25.970 21.879  1.00 29.03 ? 280 ALA A C   1 
ATOM   2239 O O   . ALA A 1 279 ? 25.680  -24.963 21.952  1.00 30.42 ? 280 ALA A O   1 
ATOM   2240 C CB  . ALA A 1 279 ? 25.809  -26.998 19.669  1.00 26.49 ? 280 ALA A CB  1 
ATOM   2241 N N   . THR A 1 280 ? 27.613  -26.028 22.392  1.00 26.68 ? 281 THR A N   1 
ATOM   2242 C CA  . THR A 1 280 ? 28.217  -24.831 22.950  1.00 27.85 ? 281 THR A CA  1 
ATOM   2243 C C   . THR A 1 280 ? 28.357  -23.762 21.864  1.00 28.72 ? 281 THR A C   1 
ATOM   2244 O O   . THR A 1 280 ? 28.320  -24.045 20.662  1.00 27.17 ? 281 THR A O   1 
ATOM   2245 C CB  . THR A 1 280 ? 29.587  -25.137 23.546  1.00 32.48 ? 281 THR A CB  1 
ATOM   2246 O OG1 . THR A 1 280 ? 30.473  -25.510 22.485  1.00 31.45 ? 281 THR A OG1 1 
ATOM   2247 C CG2 . THR A 1 280 ? 29.505  -26.280 24.570  1.00 33.31 ? 281 THR A CG2 1 
ATOM   2248 N N   . LEU A 1 281 ? 28.505  -22.512 22.301  1.00 29.42 ? 282 LEU A N   1 
ATOM   2249 C CA  . LEU A 1 281 ? 28.728  -21.434 21.339  1.00 34.55 ? 282 LEU A CA  1 
ATOM   2250 C C   . LEU A 1 281 ? 30.006  -21.674 20.530  1.00 32.69 ? 282 LEU A C   1 
ATOM   2251 O O   . LEU A 1 281 ? 30.033  -21.448 19.315  1.00 35.87 ? 282 LEU A O   1 
ATOM   2252 C CB  . LEU A 1 281 ? 28.780  -20.085 22.068  1.00 30.90 ? 282 LEU A CB  1 
ATOM   2253 C CG  . LEU A 1 281 ? 28.984  -18.837 21.204  1.00 30.34 ? 282 LEU A CG  1 
ATOM   2254 C CD1 . LEU A 1 281 ? 27.928  -18.746 20.101  1.00 30.60 ? 282 LEU A CD1 1 
ATOM   2255 C CD2 . LEU A 1 281 ? 28.990  -17.573 22.063  1.00 37.81 ? 282 LEU A CD2 1 
ATOM   2256 N N   . GLN A 1 282 ? 31.058  -22.173 21.182  1.00 31.07 ? 283 GLN A N   1 
ATOM   2257 C CA  . GLN A 1 282 ? 32.310  -22.465 20.486  1.00 36.33 ? 283 GLN A CA  1 
ATOM   2258 C C   . GLN A 1 282 ? 32.135  -23.534 19.406  1.00 36.86 ? 283 GLN A C   1 
ATOM   2259 O O   . GLN A 1 282 ? 32.690  -23.413 18.306  1.00 37.47 ? 283 GLN A O   1 
ATOM   2260 C CB  . GLN A 1 282 ? 33.369  -22.895 21.496  1.00 36.81 ? 283 GLN A CB  1 
ATOM   2261 C CG  . GLN A 1 282 ? 34.767  -22.857 20.923  1.00 46.35 ? 283 GLN A CG  1 
ATOM   2262 C CD  . GLN A 1 282 ? 35.079  -21.508 20.289  1.00 47.33 ? 283 GLN A CD  1 
ATOM   2263 O OE1 . GLN A 1 282 ? 35.248  -21.403 19.068  1.00 43.94 ? 283 GLN A OE1 1 
ATOM   2264 N NE2 . GLN A 1 282 ? 35.145  -20.467 21.113  1.00 45.31 ? 283 GLN A NE2 1 
ATOM   2265 N N   . THR A 1 283 ? 31.384  -24.598 19.697  1.00 33.94 ? 284 THR A N   1 
ATOM   2266 C CA  . THR A 1 283 ? 31.127  -25.607 18.672  1.00 34.75 ? 284 THR A CA  1 
ATOM   2267 C C   . THR A 1 283 ? 30.440  -25.004 17.447  1.00 36.73 ? 284 THR A C   1 
ATOM   2268 O O   . THR A 1 283 ? 30.781  -25.341 16.303  1.00 32.75 ? 284 THR A O   1 
ATOM   2269 C CB  . THR A 1 283 ? 30.292  -26.744 19.263  1.00 29.48 ? 284 THR A CB  1 
ATOM   2270 O OG1 . THR A 1 283 ? 31.077  -27.437 20.238  1.00 33.63 ? 284 THR A OG1 1 
ATOM   2271 C CG2 . THR A 1 283 ? 29.832  -27.710 18.180  1.00 31.78 ? 284 THR A CG2 1 
ATOM   2272 N N   . LEU A 1 284 ? 29.476  -24.101 17.660  1.00 34.77 ? 285 LEU A N   1 
ATOM   2273 C CA  . LEU A 1 284 ? 28.773  -23.508 16.525  1.00 35.69 ? 285 LEU A CA  1 
ATOM   2274 C C   . LEU A 1 284 ? 29.673  -22.536 15.767  1.00 36.70 ? 285 LEU A C   1 
ATOM   2275 O O   . LEU A 1 284 ? 29.616  -22.460 14.529  1.00 34.32 ? 285 LEU A O   1 
ATOM   2276 C CB  . LEU A 1 284 ? 27.504  -22.806 17.001  1.00 30.93 ? 285 LEU A CB  1 
ATOM   2277 C CG  . LEU A 1 284 ? 26.451  -23.709 17.635  1.00 31.69 ? 285 LEU A CG  1 
ATOM   2278 C CD1 . LEU A 1 284 ? 25.314  -22.877 18.196  1.00 30.20 ? 285 LEU A CD1 1 
ATOM   2279 C CD2 . LEU A 1 284 ? 25.921  -24.744 16.645  1.00 30.20 ? 285 LEU A CD2 1 
ATOM   2280 N N   . LEU A 1 285 ? 30.508  -21.788 16.497  1.00 33.52 ? 286 LEU A N   1 
ATOM   2281 C CA  . LEU A 1 285 ? 31.459  -20.878 15.869  1.00 35.38 ? 286 LEU A CA  1 
ATOM   2282 C C   . LEU A 1 285 ? 32.507  -21.640 15.065  1.00 42.57 ? 286 LEU A C   1 
ATOM   2283 O O   . LEU A 1 285 ? 32.912  -21.198 13.980  1.00 41.76 ? 286 LEU A O   1 
ATOM   2284 C CB  . LEU A 1 285 ? 32.133  -20.010 16.937  1.00 34.66 ? 286 LEU A CB  1 
ATOM   2285 C CG  . LEU A 1 285 ? 31.248  -18.939 17.588  1.00 36.16 ? 286 LEU A CG  1 
ATOM   2286 C CD1 . LEU A 1 285 ? 32.023  -18.141 18.633  1.00 35.41 ? 286 LEU A CD1 1 
ATOM   2287 C CD2 . LEU A 1 285 ? 30.665  -18.000 16.542  1.00 38.24 ? 286 LEU A CD2 1 
ATOM   2288 N N   . ASP A 1 286 ? 32.958  -22.785 15.586  1.00 36.92 ? 287 ASP A N   1 
ATOM   2289 C CA  . ASP A 1 286 ? 34.018  -23.539 14.925  1.00 37.32 ? 287 ASP A CA  1 
ATOM   2290 C C   . ASP A 1 286 ? 33.566  -24.098 13.585  1.00 38.60 ? 287 ASP A C   1 
ATOM   2291 O O   . ASP A 1 286 ? 34.385  -24.222 12.662  1.00 38.11 ? 287 ASP A O   1 
ATOM   2292 C CB  . ASP A 1 286 ? 34.501  -24.667 15.832  1.00 41.60 ? 287 ASP A CB  1 
ATOM   2293 C CG  . ASP A 1 286 ? 35.429  -24.174 16.926  1.00 46.12 ? 287 ASP A CG  1 
ATOM   2294 O OD1 . ASP A 1 286 ? 35.797  -22.975 16.916  1.00 44.41 ? 287 ASP A OD1 1 
ATOM   2295 O OD2 . ASP A 1 286 ? 35.792  -24.992 17.793  1.00 48.62 ? 287 ASP A OD2 1 
ATOM   2296 N N   . SER A 1 287 ? 32.273  -24.423 13.452  1.00 34.74 ? 288 SER A N   1 
ATOM   2297 C CA  . SER A 1 287 ? 31.755  -24.921 12.183  1.00 40.47 ? 288 SER A CA  1 
ATOM   2298 C C   . SER A 1 287 ? 31.924  -23.902 11.064  1.00 46.76 ? 288 SER A C   1 
ATOM   2299 O O   . SER A 1 287 ? 31.847  -24.270 9.887   1.00 42.50 ? 288 SER A O   1 
ATOM   2300 C CB  . SER A 1 287 ? 30.274  -25.293 12.317  1.00 39.76 ? 288 SER A CB  1 
ATOM   2301 O OG  . SER A 1 287 ? 29.454  -24.128 12.362  1.00 37.35 ? 288 SER A OG  1 
ATOM   2302 N N   . ASN A 1 288 ? 32.141  -22.631 11.411  1.00 51.47 ? 289 ASN A N   1 
ATOM   2303 C CA  . ASN A 1 288 ? 32.394  -21.573 10.443  1.00 53.91 ? 289 ASN A CA  1 
ATOM   2304 C C   . ASN A 1 288 ? 33.816  -21.033 10.533  1.00 50.60 ? 289 ASN A C   1 
ATOM   2305 O O   . ASN A 1 288 ? 34.071  -19.899 10.115  1.00 51.03 ? 289 ASN A O   1 
ATOM   2306 C CB  . ASN A 1 288 ? 31.381  -20.441 10.616  1.00 55.60 ? 289 ASN A CB  1 
ATOM   2307 C CG  . ASN A 1 288 ? 30.056  -20.749 9.947   1.00 63.97 ? 289 ASN A CG  1 
ATOM   2308 O OD1 . ASN A 1 288 ? 29.751  -20.214 8.878   1.00 63.51 ? 289 ASN A OD1 1 
ATOM   2309 N ND2 . ASN A 1 288 ? 29.270  -21.630 10.559  1.00 63.62 ? 289 ASN A ND2 1 
ATOM   2310 N N   . SER A 1 289 ? 34.745  -21.816 11.075  1.00 48.21 ? 290 SER A N   1 
ATOM   2311 C CA  . SER A 1 289 ? 36.138  -21.410 11.049  1.00 47.39 ? 290 SER A CA  1 
ATOM   2312 C C   . SER A 1 289 ? 36.654  -21.411 9.615   1.00 48.16 ? 290 SER A C   1 
ATOM   2313 O O   . SER A 1 289 ? 36.100  -22.065 8.719   1.00 42.42 ? 290 SER A O   1 
ATOM   2314 C CB  . SER A 1 289 ? 36.996  -22.335 11.913  1.00 44.79 ? 290 SER A CB  1 
ATOM   2315 O OG  . SER A 1 289 ? 37.110  -23.624 11.334  1.00 43.49 ? 290 SER A OG  1 
ATOM   2316 N N   . GLU A 1 290 ? 37.727  -20.648 9.404   1.00 45.42 ? 291 GLU A N   1 
ATOM   2317 C CA  . GLU A 1 290 ? 38.396  -20.645 8.108   1.00 45.90 ? 291 GLU A CA  1 
ATOM   2318 C C   . GLU A 1 290 ? 38.859  -22.050 7.738   1.00 45.61 ? 291 GLU A C   1 
ATOM   2319 O O   . GLU A 1 290 ? 38.796  -22.446 6.568   1.00 46.43 ? 291 GLU A O   1 
ATOM   2320 C CB  . GLU A 1 290 ? 39.569  -19.658 8.143   1.00 51.38 ? 291 GLU A CB  1 
ATOM   2321 C CG  . GLU A 1 290 ? 40.272  -19.424 6.812   1.00 58.83 ? 291 GLU A CG  1 
ATOM   2322 C CD  . GLU A 1 290 ? 41.279  -20.512 6.478   1.00 58.64 ? 291 GLU A CD  1 
ATOM   2323 O OE1 . GLU A 1 290 ? 41.049  -21.250 5.495   1.00 55.48 ? 291 GLU A OE1 1 
ATOM   2324 O OE2 . GLU A 1 290 ? 42.293  -20.632 7.202   1.00 58.78 ? 291 GLU A OE2 1 
ATOM   2325 N N   . GLN A 1 291 ? 39.291  -22.827 8.734   1.00 44.18 ? 292 GLN A N   1 
ATOM   2326 C CA  . GLN A 1 291 ? 39.748  -24.193 8.490   1.00 43.59 ? 292 GLN A CA  1 
ATOM   2327 C C   . GLN A 1 291 ? 38.634  -25.056 7.900   1.00 41.88 ? 292 GLN A C   1 
ATOM   2328 O O   . GLN A 1 291 ? 38.844  -25.776 6.915   1.00 40.99 ? 292 GLN A O   1 
ATOM   2329 C CB  . GLN A 1 291 ? 40.274  -24.794 9.793   1.00 41.48 ? 292 GLN A CB  1 
ATOM   2330 C CG  . GLN A 1 291 ? 40.563  -26.288 9.718   1.00 43.37 ? 292 GLN A CG  1 
ATOM   2331 C CD  . GLN A 1 291 ? 41.796  -26.603 8.888   1.00 46.57 ? 292 GLN A CD  1 
ATOM   2332 O OE1 . GLN A 1 291 ? 41.768  -27.478 8.019   1.00 46.46 ? 292 GLN A OE1 1 
ATOM   2333 N NE2 . GLN A 1 291 ? 42.889  -25.893 9.154   1.00 45.36 ? 292 GLN A NE2 1 
ATOM   2334 N N   . ILE A 1 292 ? 37.432  -24.986 8.480   1.00 41.08 ? 293 ILE A N   1 
ATOM   2335 C CA  . ILE A 1 292 ? 36.314  -25.787 7.981   1.00 38.33 ? 293 ILE A CA  1 
ATOM   2336 C C   . ILE A 1 292 ? 35.799  -25.228 6.657   1.00 41.66 ? 293 ILE A C   1 
ATOM   2337 O O   . ILE A 1 292 ? 35.461  -25.982 5.735   1.00 39.06 ? 293 ILE A O   1 
ATOM   2338 C CB  . ILE A 1 292 ? 35.198  -25.866 9.045   1.00 37.73 ? 293 ILE A CB  1 
ATOM   2339 C CG1 . ILE A 1 292 ? 35.667  -26.654 10.278  1.00 42.95 ? 293 ILE A CG1 1 
ATOM   2340 C CG2 . ILE A 1 292 ? 33.893  -26.458 8.463   1.00 38.38 ? 293 ILE A CG2 1 
ATOM   2341 C CD1 . ILE A 1 292 ? 35.972  -28.145 10.009  1.00 38.62 ? 293 ILE A CD1 1 
ATOM   2342 N N   . PHE A 1 293 ? 35.753  -23.899 6.529   1.00 41.73 ? 294 PHE A N   1 
ATOM   2343 C CA  . PHE A 1 293 ? 35.124  -23.290 5.359   1.00 43.79 ? 294 PHE A CA  1 
ATOM   2344 C C   . PHE A 1 293 ? 35.965  -23.470 4.098   1.00 43.93 ? 294 PHE A C   1 
ATOM   2345 O O   . PHE A 1 293 ? 35.416  -23.675 3.009   1.00 42.00 ? 294 PHE A O   1 
ATOM   2346 C CB  . PHE A 1 293 ? 34.862  -21.801 5.618   1.00 46.59 ? 294 PHE A CB  1 
ATOM   2347 C CG  . PHE A 1 293 ? 34.272  -21.079 4.439   1.00 51.40 ? 294 PHE A CG  1 
ATOM   2348 C CD1 . PHE A 1 293 ? 32.949  -21.300 4.061   1.00 49.58 ? 294 PHE A CD1 1 
ATOM   2349 C CD2 . PHE A 1 293 ? 35.038  -20.181 3.701   1.00 52.05 ? 294 PHE A CD2 1 
ATOM   2350 C CE1 . PHE A 1 293 ? 32.398  -20.637 2.964   1.00 49.50 ? 294 PHE A CE1 1 
ATOM   2351 C CE2 . PHE A 1 293 ? 34.496  -19.510 2.606   1.00 51.26 ? 294 PHE A CE2 1 
ATOM   2352 C CZ  . PHE A 1 293 ? 33.176  -19.738 2.235   1.00 49.83 ? 294 PHE A CZ  1 
ATOM   2353 N N   . MET A 1 294 ? 37.295  -23.408 4.219   1.00 46.73 ? 295 MET A N   1 
ATOM   2354 C CA  . MET A 1 294 ? 38.161  -23.263 3.056   1.00 46.47 ? 295 MET A CA  1 
ATOM   2355 C C   . MET A 1 294 ? 39.122  -24.417 2.804   1.00 45.87 ? 295 MET A C   1 
ATOM   2356 O O   . MET A 1 294 ? 39.625  -24.535 1.678   1.00 43.57 ? 295 MET A O   1 
ATOM   2357 C CB  . MET A 1 294 ? 38.983  -21.968 3.170   1.00 50.51 ? 295 MET A CB  1 
ATOM   2358 C CG  . MET A 1 294 ? 38.297  -20.743 2.582   1.00 58.75 ? 295 MET A CG  1 
ATOM   2359 S SD  . MET A 1 294 ? 38.527  -20.643 0.793   1.00 69.85 ? 295 MET A SD  1 
ATOM   2360 C CE  . MET A 1 294 ? 40.328  -20.604 0.704   1.00 60.37 ? 295 MET A CE  1 
ATOM   2361 N N   . LYS A 1 295 ? 39.400  -25.257 3.796   1.00 39.94 ? 296 LYS A N   1 
ATOM   2362 C CA  . LYS A 1 295 ? 40.448  -26.260 3.697   1.00 41.97 ? 296 LYS A CA  1 
ATOM   2363 C C   . LYS A 1 295 ? 39.857  -27.661 3.561   1.00 37.33 ? 296 LYS A C   1 
ATOM   2364 O O   . LYS A 1 295 ? 38.684  -27.890 3.890   1.00 32.13 ? 296 LYS A O   1 
ATOM   2365 C CB  . LYS A 1 295 ? 41.367  -26.198 4.929   1.00 42.54 ? 296 LYS A CB  1 
ATOM   2366 C CG  . LYS A 1 295 ? 42.067  -24.863 5.121   1.00 50.18 ? 296 LYS A CG  1 
ATOM   2367 C CD  . LYS A 1 295 ? 42.930  -24.493 3.916   1.00 52.14 ? 296 LYS A CD  1 
ATOM   2368 C CE  . LYS A 1 295 ? 43.744  -23.241 4.194   1.00 50.27 ? 296 LYS A CE  1 
ATOM   2369 N NZ  . LYS A 1 295 ? 44.535  -23.344 5.454   1.00 50.57 ? 296 LYS A NZ  1 
ATOM   2370 N N   . PRO A 1 296 ? 40.632  -28.618 3.040   1.00 34.43 ? 297 PRO A N   1 
ATOM   2371 C CA  . PRO A 1 296 ? 40.150  -30.008 2.985   1.00 29.26 ? 297 PRO A CA  1 
ATOM   2372 C C   . PRO A 1 296 ? 40.342  -30.658 4.346   1.00 29.00 ? 297 PRO A C   1 
ATOM   2373 O O   . PRO A 1 296 ? 41.436  -30.618 4.913   1.00 30.61 ? 297 PRO A O   1 
ATOM   2374 C CB  . PRO A 1 296 ? 41.047  -30.667 1.926   1.00 33.00 ? 297 PRO A CB  1 
ATOM   2375 C CG  . PRO A 1 296 ? 41.917  -29.562 1.373   1.00 29.95 ? 297 PRO A CG  1 
ATOM   2376 C CD  . PRO A 1 296 ? 41.941  -28.472 2.393   1.00 35.57 ? 297 PRO A CD  1 
ATOM   2377 N N   . ASN A 1 297 ? 39.275  -31.239 4.875   1.00 25.55 ? 298 ASN A N   1 
ATOM   2378 C CA  . ASN A 1 297 ? 39.315  -31.887 6.177   1.00 25.66 ? 298 ASN A CA  1 
ATOM   2379 C C   . ASN A 1 297 ? 38.916  -33.354 6.054   1.00 25.04 ? 298 ASN A C   1 
ATOM   2380 O O   . ASN A 1 297 ? 37.892  -33.679 5.448   1.00 24.00 ? 298 ASN A O   1 
ATOM   2381 C CB  . ASN A 1 297 ? 38.409  -31.157 7.163   1.00 29.08 ? 298 ASN A CB  1 
ATOM   2382 C CG  . ASN A 1 297 ? 38.885  -29.741 7.442   1.00 33.49 ? 298 ASN A CG  1 
ATOM   2383 O OD1 . ASN A 1 297 ? 39.775  -29.520 8.267   1.00 35.44 ? 298 ASN A OD1 1 
ATOM   2384 N ND2 . ASN A 1 297 ? 38.311  -28.778 6.738   1.00 33.79 ? 298 ASN A ND2 1 
ATOM   2385 N N   . LYS A 1 298 ? 39.727  -34.227 6.651   1.00 25.80 ? 299 LYS A N   1 
ATOM   2386 C CA  . LYS A 1 298 ? 39.439  -35.657 6.672   1.00 25.42 ? 299 LYS A CA  1 
ATOM   2387 C C   . LYS A 1 298 ? 38.116  -35.936 7.381   1.00 24.39 ? 299 LYS A C   1 
ATOM   2388 O O   . LYS A 1 298 ? 37.884  -35.459 8.496   1.00 24.49 ? 299 LYS A O   1 
ATOM   2389 C CB  . LYS A 1 298 ? 40.580  -36.386 7.378   1.00 26.60 ? 299 LYS A CB  1 
ATOM   2390 C CG  . LYS A 1 298 ? 40.408  -37.893 7.478   1.00 28.24 ? 299 LYS A CG  1 
ATOM   2391 C CD  . LYS A 1 298 ? 40.468  -38.556 6.122   1.00 26.99 ? 299 LYS A CD  1 
ATOM   2392 C CE  . LYS A 1 298 ? 40.845  -40.041 6.255   1.00 34.45 ? 299 LYS A CE  1 
ATOM   2393 N NZ  . LYS A 1 298 ? 42.181  -40.187 6.885   1.00 46.25 ? 299 LYS A NZ  1 
ATOM   2394 N N   . VAL A 1 299 ? 37.253  -36.739 6.742   1.00 23.54 ? 300 VAL A N   1 
ATOM   2395 C CA  . VAL A 1 299 ? 35.975  -37.128 7.324   1.00 22.67 ? 300 VAL A CA  1 
ATOM   2396 C C   . VAL A 1 299 ? 36.119  -38.479 8.026   1.00 23.02 ? 300 VAL A C   1 
ATOM   2397 O O   . VAL A 1 299 ? 36.994  -39.290 7.718   1.00 23.68 ? 300 VAL A O   1 
ATOM   2398 C CB  . VAL A 1 299 ? 34.831  -37.168 6.261   1.00 21.65 ? 300 VAL A CB  1 
ATOM   2399 C CG1 . VAL A 1 299 ? 34.941  -35.991 5.292   1.00 21.55 ? 300 VAL A CG1 1 
ATOM   2400 C CG2 . VAL A 1 299 ? 34.815  -38.481 5.490   1.00 21.61 ? 300 VAL A CG2 1 
ATOM   2401 N N   . THR A 1 300 ? 35.248  -38.725 9.004   1.00 22.67 ? 301 THR A N   1 
ATOM   2402 C CA  . THR A 1 300 ? 35.194  -40.017 9.678   1.00 23.40 ? 301 THR A CA  1 
ATOM   2403 C C   . THR A 1 300 ? 33.773  -40.569 9.620   1.00 25.16 ? 301 THR A C   1 
ATOM   2404 O O   . THR A 1 300 ? 32.798  -39.831 9.777   1.00 21.80 ? 301 THR A O   1 
ATOM   2405 C CB  . THR A 1 300 ? 35.667  -39.914 11.137  1.00 25.97 ? 301 THR A CB  1 
ATOM   2406 O OG1 . THR A 1 300 ? 34.788  -39.056 11.855  1.00 34.62 ? 301 THR A OG1 1 
ATOM   2407 C CG2 . THR A 1 300 ? 37.047  -39.305 11.221  1.00 24.80 ? 301 THR A CG2 1 
ATOM   2408 N N   . ALA A 1 301 ? 33.655  -41.876 9.390   1.00 25.50 ? 302 ALA A N   1 
ATOM   2409 C CA  . ALA A 1 301 ? 32.333  -42.492 9.361   1.00 28.49 ? 302 ALA A CA  1 
ATOM   2410 C C   . ALA A 1 301 ? 31.646  -42.343 10.717  1.00 28.68 ? 302 ALA A C   1 
ATOM   2411 O O   . ALA A 1 301 ? 32.288  -42.328 11.771  1.00 26.73 ? 302 ALA A O   1 
ATOM   2412 C CB  . ALA A 1 301 ? 32.440  -43.975 8.984   1.00 31.83 ? 302 ALA A CB  1 
ATOM   2413 N N   . ILE A 1 302 ? 30.321  -42.234 10.685  1.00 30.44 ? 303 ILE A N   1 
ATOM   2414 C CA  . ILE A 1 302 ? 29.553  -42.061 11.911  1.00 32.93 ? 303 ILE A CA  1 
ATOM   2415 C C   . ILE A 1 302 ? 29.330  -43.417 12.567  1.00 40.60 ? 303 ILE A C   1 
ATOM   2416 O O   . ILE A 1 302 ? 28.949  -44.385 11.899  1.00 45.61 ? 303 ILE A O   1 
ATOM   2417 C CB  . ILE A 1 302 ? 28.219  -41.367 11.614  1.00 37.59 ? 303 ILE A CB  1 
ATOM   2418 C CG1 . ILE A 1 302 ? 28.465  -39.894 11.276  1.00 29.47 ? 303 ILE A CG1 1 
ATOM   2419 C CG2 . ILE A 1 302 ? 27.265  -41.525 12.784  1.00 37.06 ? 303 ILE A CG2 1 
ATOM   2420 C CD1 . ILE A 1 302 ? 27.273  -39.231 10.671  1.00 27.26 ? 303 ILE A CD1 1 
ATOM   2421 N N   . SER A 1 303 ? 29.577  -43.492 13.875  1.00 47.52 ? 304 SER A N   1 
ATOM   2422 C CA  . SER A 1 303 ? 29.299  -44.699 14.647  1.00 55.49 ? 304 SER A CA  1 
ATOM   2423 C C   . SER A 1 303 ? 27.795  -44.840 14.841  1.00 55.53 ? 304 SER A C   1 
ATOM   2424 O O   . SER A 1 303 ? 27.162  -45.722 14.252  1.00 56.43 ? 304 SER A O   1 
ATOM   2425 C CB  . SER A 1 303 ? 30.012  -44.655 16.002  1.00 58.53 ? 304 SER A CB  1 
ATOM   2426 O OG  . SER A 1 303 ? 29.418  -43.690 16.856  1.00 65.09 ? 304 SER A OG  1 
ATOM   2427 N N   . LYS A 1 304 ? 27.223  -43.978 15.679  1.00 49.91 ? 305 LYS A N   1 
ATOM   2428 C CA  . LYS A 1 304 ? 25.788  -43.739 15.713  1.00 52.57 ? 305 LYS A CA  1 
ATOM   2429 C C   . LYS A 1 304 ? 25.554  -42.234 15.747  1.00 45.57 ? 305 LYS A C   1 
ATOM   2430 O O   . LYS A 1 304 ? 26.368  -41.478 16.288  1.00 44.40 ? 305 LYS A O   1 
ATOM   2431 C CB  . LYS A 1 304 ? 25.109  -44.421 16.919  1.00 55.77 ? 305 LYS A CB  1 
ATOM   2432 C CG  . LYS A 1 304 ? 25.634  -43.986 18.283  1.00 56.91 ? 305 LYS A CG  1 
ATOM   2433 C CD  . LYS A 1 304 ? 24.805  -44.586 19.416  1.00 62.74 ? 305 LYS A CD  1 
ATOM   2434 C CE  . LYS A 1 304 ? 23.375  -44.054 19.414  1.00 66.03 ? 305 LYS A CE  1 
ATOM   2435 N NZ  . LYS A 1 304 ? 22.544  -44.640 20.504  1.00 65.84 ? 305 LYS A NZ  1 
ATOM   2436 N N   . GLU A 1 305 ? 24.451  -41.803 15.136  1.00 43.09 ? 306 GLU A N   1 
ATOM   2437 C CA  A GLU A 1 305 ? 24.129  -40.387 15.137  0.45 38.96 ? 306 GLU A CA  1 
ATOM   2438 C CA  B GLU A 1 305 ? 24.092  -40.393 15.134  0.55 39.17 ? 306 GLU A CA  1 
ATOM   2439 C C   . GLU A 1 305 ? 23.881  -39.911 16.569  1.00 37.15 ? 306 GLU A C   1 
ATOM   2440 O O   . GLU A 1 305 ? 23.524  -40.704 17.450  1.00 35.88 ? 306 GLU A O   1 
ATOM   2441 C CB  A GLU A 1 305 ? 22.908  -40.113 14.255  0.45 39.36 ? 306 GLU A CB  1 
ATOM   2442 C CB  B GLU A 1 305 ? 22.816  -40.170 14.318  0.55 39.40 ? 306 GLU A CB  1 
ATOM   2443 C CG  A GLU A 1 305 ? 23.118  -38.981 13.241  0.45 33.64 ? 306 GLU A CG  1 
ATOM   2444 C CG  B GLU A 1 305 ? 22.762  -40.909 12.976  0.55 36.84 ? 306 GLU A CG  1 
ATOM   2445 C CD  A GLU A 1 305 ? 22.027  -38.905 12.192  0.45 33.13 ? 306 GLU A CD  1 
ATOM   2446 C CD  B GLU A 1 305 ? 23.568  -40.227 11.883  0.55 32.04 ? 306 GLU A CD  1 
ATOM   2447 O OE1 A GLU A 1 305 ? 21.661  -39.963 11.629  0.45 34.76 ? 306 GLU A OE1 1 
ATOM   2448 O OE1 B GLU A 1 305 ? 24.125  -39.139 12.145  0.55 30.17 ? 306 GLU A OE1 1 
ATOM   2449 O OE2 A GLU A 1 305 ? 21.527  -37.789 11.932  0.45 30.07 ? 306 GLU A OE2 1 
ATOM   2450 O OE2 B GLU A 1 305 ? 23.642  -40.781 10.762  0.55 29.37 ? 306 GLU A OE2 1 
ATOM   2451 N N   . PRO A 1 306 ? 24.101  -38.624 16.848  1.00 34.91 ? 307 PRO A N   1 
ATOM   2452 C CA  . PRO A 1 306 ? 23.805  -38.119 18.192  1.00 33.75 ? 307 PRO A CA  1 
ATOM   2453 C C   . PRO A 1 306 ? 22.321  -38.271 18.483  1.00 33.84 ? 307 PRO A C   1 
ATOM   2454 O O   . PRO A 1 306 ? 21.482  -38.214 17.586  1.00 33.81 ? 307 PRO A O   1 
ATOM   2455 C CB  . PRO A 1 306 ? 24.220  -36.644 18.127  1.00 33.59 ? 307 PRO A CB  1 
ATOM   2456 C CG  . PRO A 1 306 ? 24.216  -36.314 16.681  1.00 34.99 ? 307 PRO A CG  1 
ATOM   2457 C CD  . PRO A 1 306 ? 24.650  -37.566 15.981  1.00 36.14 ? 307 PRO A CD  1 
ATOM   2458 N N   . SER A 1 307 ? 22.009  -38.498 19.755  1.00 30.96 ? 308 SER A N   1 
ATOM   2459 C CA  . SER A 1 307 ? 20.639  -38.825 20.132  1.00 33.44 ? 308 SER A CA  1 
ATOM   2460 C C   . SER A 1 307 ? 19.718  -37.615 20.010  1.00 34.71 ? 308 SER A C   1 
ATOM   2461 O O   . SER A 1 307 ? 18.552  -37.754 19.621  1.00 34.35 ? 308 SER A O   1 
ATOM   2462 C CB  . SER A 1 307 ? 20.631  -39.390 21.552  1.00 37.97 ? 308 SER A CB  1 
ATOM   2463 O OG  . SER A 1 307 ? 19.312  -39.631 21.990  1.00 47.38 ? 308 SER A OG  1 
ATOM   2464 N N   . VAL A 1 308 ? 20.216  -36.425 20.341  1.00 30.08 ? 309 VAL A N   1 
ATOM   2465 C CA  . VAL A 1 308 ? 19.443  -35.190 20.273  1.00 30.21 ? 309 VAL A CA  1 
ATOM   2466 C C   . VAL A 1 308 ? 20.247  -34.212 19.431  1.00 26.37 ? 309 VAL A C   1 
ATOM   2467 O O   . VAL A 1 308 ? 21.448  -34.033 19.661  1.00 22.50 ? 309 VAL A O   1 
ATOM   2468 C CB  . VAL A 1 308 ? 19.146  -34.613 21.673  1.00 34.55 ? 309 VAL A CB  1 
ATOM   2469 C CG1 . VAL A 1 308 ? 18.057  -33.555 21.591  1.00 32.24 ? 309 VAL A CG1 1 
ATOM   2470 C CG2 . VAL A 1 308 ? 18.719  -35.719 22.637  1.00 33.88 ? 309 VAL A CG2 1 
ATOM   2471 N N   . LYS A 1 309 ? 19.600  -33.602 18.440  1.00 26.10 ? 310 LYS A N   1 
ATOM   2472 C CA  . LYS A 1 309 ? 20.317  -32.884 17.403  1.00 24.55 ? 310 LYS A CA  1 
ATOM   2473 C C   . LYS A 1 309 ? 19.793  -31.464 17.256  1.00 27.66 ? 310 LYS A C   1 
ATOM   2474 O O   . LYS A 1 309 ? 18.654  -31.152 17.611  1.00 27.13 ? 310 LYS A O   1 
ATOM   2475 C CB  . LYS A 1 309 ? 20.191  -33.574 16.032  1.00 29.33 ? 310 LYS A CB  1 
ATOM   2476 C CG  . LYS A 1 309 ? 20.821  -34.955 15.928  1.00 37.40 ? 310 LYS A CG  1 
ATOM   2477 C CD  . LYS A 1 309 ? 19.738  -36.022 15.803  1.00 37.63 ? 310 LYS A CD  1 
ATOM   2478 C CE  . LYS A 1 309 ? 20.240  -37.271 15.087  1.00 39.01 ? 310 LYS A CE  1 
ATOM   2479 N NZ  . LYS A 1 309 ? 19.655  -38.505 15.685  1.00 41.48 ? 310 LYS A NZ  1 
ATOM   2480 N N   . MET A 1 310 ? 20.651  -30.613 16.711  1.00 24.28 ? 311 MET A N   1 
ATOM   2481 C CA  . MET A 1 310 ? 20.227  -29.347 16.138  1.00 23.75 ? 311 MET A CA  1 
ATOM   2482 C C   . MET A 1 310 ? 20.960  -29.141 14.819  1.00 21.95 ? 311 MET A C   1 
ATOM   2483 O O   . MET A 1 310 ? 21.919  -29.848 14.504  1.00 24.09 ? 311 MET A O   1 
ATOM   2484 C CB  . MET A 1 310 ? 20.502  -28.193 17.092  1.00 27.57 ? 311 MET A CB  1 
ATOM   2485 C CG  . MET A 1 310 ? 21.977  -28.042 17.361  1.00 28.11 ? 311 MET A CG  1 
ATOM   2486 S SD  . MET A 1 310 ? 22.225  -26.657 18.449  1.00 43.76 ? 311 MET A SD  1 
ATOM   2487 C CE  . MET A 1 310 ? 22.331  -25.319 17.257  1.00 33.44 ? 311 MET A CE  1 
ATOM   2488 N N   . TYR A 1 311 ? 20.511  -28.145 14.051  1.00 21.32 ? 312 TYR A N   1 
ATOM   2489 C CA  . TYR A 1 311 ? 20.890  -28.004 12.654  1.00 20.98 ? 312 TYR A CA  1 
ATOM   2490 C C   . TYR A 1 311 ? 21.012  -26.523 12.341  1.00 20.66 ? 312 TYR A C   1 
ATOM   2491 O O   . TYR A 1 311 ? 20.187  -25.747 12.812  1.00 20.45 ? 312 TYR A O   1 
ATOM   2492 C CB  . TYR A 1 311 ? 19.813  -28.608 11.719  1.00 20.71 ? 312 TYR A CB  1 
ATOM   2493 C CG  . TYR A 1 311 ? 19.515  -30.068 11.945  1.00 21.16 ? 312 TYR A CG  1 
ATOM   2494 C CD1 . TYR A 1 311 ? 18.640  -30.481 12.952  1.00 21.51 ? 312 TYR A CD1 1 
ATOM   2495 C CD2 . TYR A 1 311 ? 20.090  -31.030 11.143  1.00 22.10 ? 312 TYR A CD2 1 
ATOM   2496 C CE1 . TYR A 1 311 ? 18.368  -31.836 13.155  1.00 24.92 ? 312 TYR A CE1 1 
ATOM   2497 C CE2 . TYR A 1 311 ? 19.825  -32.371 11.334  1.00 26.53 ? 312 TYR A CE2 1 
ATOM   2498 C CZ  . TYR A 1 311 ? 18.958  -32.768 12.328  1.00 23.37 ? 312 TYR A CZ  1 
ATOM   2499 O OH  . TYR A 1 311 ? 18.729  -34.123 12.493  1.00 25.34 ? 312 TYR A OH  1 
ATOM   2500 N N   . HIS A 1 312 ? 22.001  -26.129 11.534  1.00 20.74 ? 313 HIS A N   1 
ATOM   2501 C CA  . HIS A 1 312 ? 21.993  -24.756 11.034  1.00 20.57 ? 313 HIS A CA  1 
ATOM   2502 C C   . HIS A 1 312 ? 22.657  -24.677 9.662   1.00 20.72 ? 313 HIS A C   1 
ATOM   2503 O O   . HIS A 1 312 ? 23.253  -25.638 9.169   1.00 20.98 ? 313 HIS A O   1 
ATOM   2504 C CB  . HIS A 1 312 ? 22.630  -23.774 12.047  1.00 20.90 ? 313 HIS A CB  1 
ATOM   2505 C CG  . HIS A 1 312 ? 24.136  -23.765 12.078  1.00 23.51 ? 313 HIS A CG  1 
ATOM   2506 N ND1 . HIS A 1 312 ? 24.841  -22.983 12.971  1.00 22.82 ? 313 HIS A ND1 1 
ATOM   2507 C CD2 . HIS A 1 312 ? 25.067  -24.402 11.325  1.00 24.17 ? 313 HIS A CD2 1 
ATOM   2508 C CE1 . HIS A 1 312 ? 26.139  -23.147 12.775  1.00 25.92 ? 313 HIS A CE1 1 
ATOM   2509 N NE2 . HIS A 1 312 ? 26.304  -24.005 11.783  1.00 24.38 ? 313 HIS A NE2 1 
ATOM   2510 N N   . LYS A 1 313 ? 22.540  -23.502 9.045   1.00 20.69 ? 314 LYS A N   1 
ATOM   2511 C CA  . LYS A 1 313 ? 23.232  -23.214 7.798   1.00 21.08 ? 314 LYS A CA  1 
ATOM   2512 C C   . LYS A 1 313 ? 23.484  -21.713 7.720   1.00 21.38 ? 314 LYS A C   1 
ATOM   2513 O O   . LYS A 1 313 ? 22.596  -20.915 8.027   1.00 21.05 ? 314 LYS A O   1 
ATOM   2514 C CB  . LYS A 1 313 ? 22.413  -23.663 6.580   1.00 20.86 ? 314 LYS A CB  1 
ATOM   2515 C CG  . LYS A 1 313 ? 23.142  -23.483 5.243   1.00 21.46 ? 314 LYS A CG  1 
ATOM   2516 C CD  . LYS A 1 313 ? 24.193  -24.576 5.049   1.00 25.34 ? 314 LYS A CD  1 
ATOM   2517 C CE  . LYS A 1 313 ? 25.017  -24.398 3.778   1.00 30.78 ? 314 LYS A CE  1 
ATOM   2518 N NZ  . LYS A 1 313 ? 25.980  -23.245 3.864   1.00 33.66 ? 314 LYS A NZ  1 
ATOM   2519 N N   . THR A 1 314 ? 24.694  -21.336 7.316   1.00 22.39 ? 315 THR A N   1 
ATOM   2520 C CA  . THR A 1 314 ? 24.998  -19.934 7.055   1.00 29.64 ? 315 THR A CA  1 
ATOM   2521 C C   . THR A 1 314 ? 24.927  -19.660 5.555   1.00 35.21 ? 315 THR A C   1 
ATOM   2522 O O   . THR A 1 314 ? 25.212  -20.533 4.729   1.00 27.35 ? 315 THR A O   1 
ATOM   2523 C CB  . THR A 1 314 ? 26.376  -19.556 7.602   1.00 37.32 ? 315 THR A CB  1 
ATOM   2524 O OG1 . THR A 1 314 ? 27.387  -20.296 6.909   1.00 39.54 ? 315 THR A OG1 1 
ATOM   2525 C CG2 . THR A 1 314 ? 26.455  -19.889 9.087   1.00 38.47 ? 315 THR A CG2 1 
ATOM   2526 N N   . GLY A 1 315 ? 24.527  -18.437 5.213   1.00 35.32 ? 316 GLY A N   1 
ATOM   2527 C CA  . GLY A 1 315 ? 24.300  -18.052 3.831   1.00 38.82 ? 316 GLY A CA  1 
ATOM   2528 C C   . GLY A 1 315 ? 25.263  -16.975 3.388   1.00 54.00 ? 316 GLY A C   1 
ATOM   2529 O O   . GLY A 1 315 ? 24.864  -15.967 2.792   1.00 49.20 ? 316 GLY A O   1 
ATOM   2530 N N   . THR A 1 316 ? 26.542  -17.219 3.686   1.00 83.28 ? 317 THR A N   1 
ATOM   2531 C CA  . THR A 1 316 ? 27.675  -16.317 3.503   1.00 90.76 ? 317 THR A CA  1 
ATOM   2532 C C   . THR A 1 316 ? 27.581  -15.433 2.265   1.00 92.39 ? 317 THR A C   1 
ATOM   2533 O O   . THR A 1 316 ? 26.941  -14.375 2.300   1.00 88.31 ? 317 THR A O   1 
ATOM   2534 C CB  . THR A 1 316 ? 28.962  -17.142 3.441   1.00 94.58 ? 317 THR A CB  1 
ATOM   2535 O OG1 . THR A 1 316 ? 29.063  -17.768 2.156   1.00 94.92 ? 317 THR A OG1 1 
ATOM   2536 C CG2 . THR A 1 316 ? 28.932  -18.229 4.500   1.00 87.05 ? 317 THR A CG2 1 
ATOM   2537 N N   . THR A 1 317 ? 28.236  -15.860 1.178   1.00 82.30 ? 318 THR A N   1 
ATOM   2538 C CA  . THR A 1 317 ? 28.314  -15.113 -0.076  1.00 80.19 ? 318 THR A CA  1 
ATOM   2539 C C   . THR A 1 317 ? 28.636  -13.641 0.164   1.00 82.90 ? 318 THR A C   1 
ATOM   2540 O O   . THR A 1 317 ? 29.497  -13.307 0.986   1.00 86.86 ? 318 THR A O   1 
ATOM   2541 C CB  . THR A 1 317 ? 27.006  -15.243 -0.866  1.00 71.24 ? 318 THR A CB  1 
ATOM   2542 O OG1 . THR A 1 317 ? 25.937  -14.616 -0.143  1.00 63.09 ? 318 THR A OG1 1 
ATOM   2543 C CG2 . THR A 1 317 ? 26.669  -16.715 -1.112  1.00 61.01 ? 318 THR A CG2 1 
ATOM   2544 N N   . ASN A 1 318 ? 27.958  -12.757 -0.561  1.00 80.38 ? 319 ASN A N   1 
ATOM   2545 C CA  . ASN A 1 318 ? 27.995  -11.330 -0.285  1.00 77.95 ? 319 ASN A CA  1 
ATOM   2546 C C   . ASN A 1 318 ? 26.689  -10.734 -0.794  1.00 71.84 ? 319 ASN A C   1 
ATOM   2547 O O   . ASN A 1 318 ? 25.834  -11.443 -1.338  1.00 70.53 ? 319 ASN A O   1 
ATOM   2548 C CB  . ASN A 1 318 ? 29.239  -10.665 -0.899  1.00 81.22 ? 319 ASN A CB  1 
ATOM   2549 C CG  . ASN A 1 318 ? 29.213  -10.633 -2.420  1.00 82.27 ? 319 ASN A CG  1 
ATOM   2550 O OD1 . ASN A 1 318 ? 28.610  -11.489 -3.067  1.00 83.82 ? 319 ASN A OD1 1 
ATOM   2551 N ND2 . ASN A 1 318 ? 29.880  -9.641  -2.997  1.00 81.08 ? 319 ASN A ND2 1 
ATOM   2552 N N   . ARG A 1 319 ? 26.526  -9.427  -0.590  1.00 71.57 ? 320 ARG A N   1 
ATOM   2553 C CA  . ARG A 1 319 ? 25.299  -8.690  -0.882  1.00 64.68 ? 320 ARG A CA  1 
ATOM   2554 C C   . ARG A 1 319 ? 24.099  -9.214  -0.101  1.00 63.43 ? 320 ARG A C   1 
ATOM   2555 O O   . ARG A 1 319 ? 22.967  -8.771  -0.334  1.00 61.12 ? 320 ARG A O   1 
ATOM   2556 C CB  . ARG A 1 319 ? 24.984  -8.693  -2.381  1.00 64.61 ? 320 ARG A CB  1 
ATOM   2557 C CG  . ARG A 1 319 ? 26.088  -8.106  -3.236  1.00 68.78 ? 320 ARG A CG  1 
ATOM   2558 C CD  . ARG A 1 319 ? 26.448  -9.048  -4.371  1.00 76.72 ? 320 ARG A CD  1 
ATOM   2559 N NE  . ARG A 1 319 ? 25.263  -9.674  -4.947  1.00 81.46 ? 320 ARG A NE  1 
ATOM   2560 C CZ  . ARG A 1 319 ? 25.260  -10.386 -6.066  1.00 81.16 ? 320 ARG A CZ  1 
ATOM   2561 N NH1 . ARG A 1 319 ? 26.360  -10.546 -6.784  1.00 82.15 ? 320 ARG A NH1 1 
ATOM   2562 N NH2 . ARG A 1 319 ? 24.126  -10.953 -6.472  1.00 72.26 ? 320 ARG A NH2 1 
ATOM   2563 N N   . SER A 1 320 ? 24.314  -10.151 0.816   1.00 53.87 ? 321 SER A N   1 
ATOM   2564 C CA  . SER A 1 320 ? 23.247  -10.646 1.667   1.00 47.59 ? 321 SER A CA  1 
ATOM   2565 C C   . SER A 1 320 ? 23.869  -11.397 2.834   1.00 44.66 ? 321 SER A C   1 
ATOM   2566 O O   . SER A 1 320 ? 25.000  -11.890 2.752   1.00 48.17 ? 321 SER A O   1 
ATOM   2567 C CB  . SER A 1 320 ? 22.277  -11.556 0.902   1.00 47.09 ? 321 SER A CB  1 
ATOM   2568 O OG  . SER A 1 320 ? 22.923  -12.741 0.460   1.00 49.54 ? 321 SER A OG  1 
ATOM   2569 N N   . GLY A 1 321 ? 23.123  -11.446 3.929   1.00 35.82 ? 322 GLY A N   1 
ATOM   2570 C CA  . GLY A 1 321 ? 23.435  -12.304 5.045   1.00 34.12 ? 322 GLY A CA  1 
ATOM   2571 C C   . GLY A 1 321 ? 22.205  -13.138 5.306   1.00 36.41 ? 322 GLY A C   1 
ATOM   2572 O O   . GLY A 1 321 ? 21.085  -12.609 5.287   1.00 33.29 ? 322 GLY A O   1 
ATOM   2573 N N   . THR A 1 322 ? 22.389  -14.442 5.484   1.00 28.74 ? 323 THR A N   1 
ATOM   2574 C CA  . THR A 1 322 ? 21.301  -15.343 5.812   1.00 25.49 ? 323 THR A CA  1 
ATOM   2575 C C   . THR A 1 322 ? 21.801  -16.283 6.891   1.00 23.37 ? 323 THR A C   1 
ATOM   2576 O O   . THR A 1 322 ? 22.959  -16.707 6.861   1.00 24.54 ? 323 THR A O   1 
ATOM   2577 C CB  . THR A 1 322 ? 20.837  -16.142 4.583   1.00 28.06 ? 323 THR A CB  1 
ATOM   2578 O OG1 . THR A 1 322 ? 20.598  -15.242 3.494   1.00 29.81 ? 323 THR A OG1 1 
ATOM   2579 C CG2 . THR A 1 322 ? 19.542  -16.904 4.885   1.00 25.63 ? 323 THR A CG2 1 
ATOM   2580 N N   . TYR A 1 323 ? 20.941  -16.591 7.846   1.00 22.19 ? 324 TYR A N   1 
ATOM   2581 C CA  . TYR A 1 323 ? 21.250  -17.620 8.826   1.00 21.13 ? 324 TYR A CA  1 
ATOM   2582 C C   . TYR A 1 323 ? 19.958  -18.312 9.215   1.00 20.41 ? 324 TYR A C   1 
ATOM   2583 O O   . TYR A 1 323 ? 18.953  -17.649 9.469   1.00 20.22 ? 324 TYR A O   1 
ATOM   2584 C CB  . TYR A 1 323 ? 21.930  -17.036 10.075  1.00 21.55 ? 324 TYR A CB  1 
ATOM   2585 C CG  . TYR A 1 323 ? 22.317  -18.078 11.100  1.00 21.64 ? 324 TYR A CG  1 
ATOM   2586 C CD1 . TYR A 1 323 ? 23.311  -19.007 10.826  1.00 23.83 ? 324 TYR A CD1 1 
ATOM   2587 C CD2 . TYR A 1 323 ? 21.714  -18.119 12.344  1.00 22.51 ? 324 TYR A CD2 1 
ATOM   2588 C CE1 . TYR A 1 323 ? 23.686  -19.973 11.774  1.00 23.83 ? 324 TYR A CE1 1 
ATOM   2589 C CE2 . TYR A 1 323 ? 22.088  -19.066 13.300  1.00 21.63 ? 324 TYR A CE2 1 
ATOM   2590 C CZ  . TYR A 1 323 ? 23.068  -19.986 13.014  1.00 22.96 ? 324 TYR A CZ  1 
ATOM   2591 O OH  . TYR A 1 323 ? 23.418  -20.937 13.959  1.00 21.73 ? 324 TYR A OH  1 
ATOM   2592 N N   . VAL A 1 324 ? 19.991  -19.646 9.293   1.00 20.15 ? 325 VAL A N   1 
ATOM   2593 C CA  . VAL A 1 324 ? 18.833  -20.421 9.722   1.00 19.68 ? 325 VAL A CA  1 
ATOM   2594 C C   . VAL A 1 324 ? 19.313  -21.492 10.702  1.00 19.76 ? 325 VAL A C   1 
ATOM   2595 O O   . VAL A 1 324 ? 20.402  -22.051 10.536  1.00 20.03 ? 325 VAL A O   1 
ATOM   2596 C CB  . VAL A 1 324 ? 18.091  -21.050 8.518   1.00 19.44 ? 325 VAL A CB  1 
ATOM   2597 C CG1 . VAL A 1 324 ? 17.543  -19.959 7.592   1.00 20.84 ? 325 VAL A CG1 1 
ATOM   2598 C CG2 . VAL A 1 324 ? 18.999  -21.993 7.759   1.00 21.03 ? 325 VAL A CG2 1 
ATOM   2599 N N   . VAL A 1 325 ? 18.512  -21.762 11.729  1.00 19.67 ? 326 VAL A N   1 
ATOM   2600 C CA  . VAL A 1 325 ? 18.851  -22.767 12.736  1.00 19.91 ? 326 VAL A CA  1 
ATOM   2601 C C   . VAL A 1 325 ? 17.567  -23.371 13.289  1.00 19.85 ? 326 VAL A C   1 
ATOM   2602 O O   . VAL A 1 325 ? 16.562  -22.681 13.434  1.00 20.58 ? 326 VAL A O   1 
ATOM   2603 C CB  . VAL A 1 325 ? 19.710  -22.157 13.870  1.00 20.36 ? 326 VAL A CB  1 
ATOM   2604 C CG1 . VAL A 1 325 ? 19.017  -20.978 14.499  1.00 20.98 ? 326 VAL A CG1 1 
ATOM   2605 C CG2 . VAL A 1 325 ? 20.031  -23.218 14.933  1.00 20.77 ? 326 VAL A CG2 1 
ATOM   2606 N N   . PHE A 1 326 ? 17.589  -24.665 13.622  1.00 20.08 ? 327 PHE A N   1 
ATOM   2607 C CA  . PHE A 1 326 ? 16.423  -25.199 14.316  1.00 20.29 ? 327 PHE A CA  1 
ATOM   2608 C C   . PHE A 1 326 ? 16.841  -26.321 15.260  1.00 20.90 ? 327 PHE A C   1 
ATOM   2609 O O   . PHE A 1 326 ? 17.886  -26.956 15.088  1.00 21.04 ? 327 PHE A O   1 
ATOM   2610 C CB  . PHE A 1 326 ? 15.321  -25.651 13.333  1.00 20.05 ? 327 PHE A CB  1 
ATOM   2611 C CG  . PHE A 1 326 ? 15.655  -26.893 12.523  1.00 20.11 ? 327 PHE A CG  1 
ATOM   2612 C CD1 . PHE A 1 326 ? 16.346  -26.790 11.318  1.00 19.83 ? 327 PHE A CD1 1 
ATOM   2613 C CD2 . PHE A 1 326 ? 15.221  -28.157 12.934  1.00 20.65 ? 327 PHE A CD2 1 
ATOM   2614 C CE1 . PHE A 1 326 ? 16.633  -27.927 10.551  1.00 19.99 ? 327 PHE A CE1 1 
ATOM   2615 C CE2 . PHE A 1 326 ? 15.507  -29.302 12.179  1.00 20.78 ? 327 PHE A CE2 1 
ATOM   2616 C CZ  . PHE A 1 326 ? 16.219  -29.189 10.989  1.00 20.44 ? 327 PHE A CZ  1 
ATOM   2617 N N   . ILE A 1 327 ? 16.014  -26.523 16.286  1.00 21.39 ? 328 ILE A N   1 
ATOM   2618 C CA  . ILE A 1 327 ? 16.222  -27.502 17.360  1.00 22.98 ? 328 ILE A CA  1 
ATOM   2619 C C   . ILE A 1 327 ? 14.951  -28.320 17.553  1.00 26.11 ? 328 ILE A C   1 
ATOM   2620 O O   . ILE A 1 327 ? 14.005  -27.849 18.212  1.00 24.66 ? 328 ILE A O   1 
ATOM   2621 C CB  . ILE A 1 327 ? 16.593  -26.830 18.695  1.00 25.00 ? 328 ILE A CB  1 
ATOM   2622 C CG1 . ILE A 1 327 ? 17.766  -25.860 18.533  1.00 27.06 ? 328 ILE A CG1 1 
ATOM   2623 C CG2 . ILE A 1 327 ? 16.903  -27.898 19.740  1.00 30.06 ? 328 ILE A CG2 1 
ATOM   2624 C CD1 . ILE A 1 327 ? 17.853  -24.818 19.650  1.00 30.60 ? 328 ILE A CD1 1 
ATOM   2625 N N   . PRO A 1 328 ? 14.885  -29.539 17.009  1.00 23.94 ? 329 PRO A N   1 
ATOM   2626 C CA  . PRO A 1 328 ? 13.647  -30.332 17.124  1.00 28.46 ? 329 PRO A CA  1 
ATOM   2627 C C   . PRO A 1 328 ? 13.196  -30.563 18.558  1.00 28.73 ? 329 PRO A C   1 
ATOM   2628 O O   . PRO A 1 328 ? 11.997  -30.453 18.837  1.00 30.24 ? 329 PRO A O   1 
ATOM   2629 C CB  . PRO A 1 328 ? 14.017  -31.648 16.420  1.00 27.75 ? 329 PRO A CB  1 
ATOM   2630 C CG  . PRO A 1 328 ? 15.049  -31.214 15.404  1.00 29.18 ? 329 PRO A CG  1 
ATOM   2631 C CD  . PRO A 1 328 ? 15.854  -30.137 16.074  1.00 24.52 ? 329 PRO A CD  1 
ATOM   2632 N N   . LYS A 1 329 ? 14.131  -30.847 19.471  1.00 28.26 ? 330 LYS A N   1 
ATOM   2633 C CA  . LYS A 1 329 ? 13.797  -31.084 20.878  1.00 34.68 ? 330 LYS A CA  1 
ATOM   2634 C C   . LYS A 1 329 ? 12.983  -29.937 21.466  1.00 35.49 ? 330 LYS A C   1 
ATOM   2635 O O   . LYS A 1 329 ? 12.097  -30.151 22.301  1.00 34.66 ? 330 LYS A O   1 
ATOM   2636 C CB  . LYS A 1 329 ? 15.091  -31.277 21.685  1.00 35.18 ? 330 LYS A CB  1 
ATOM   2637 C CG  . LYS A 1 329 ? 14.944  -31.202 23.205  1.00 44.08 ? 330 LYS A CG  1 
ATOM   2638 C CD  . LYS A 1 329 ? 14.797  -32.576 23.831  1.00 41.23 ? 330 LYS A CD  1 
ATOM   2639 C CE  . LYS A 1 329 ? 14.576  -32.471 25.333  1.00 47.01 ? 330 LYS A CE  1 
ATOM   2640 N NZ  . LYS A 1 329 ? 14.402  -33.806 25.960  1.00 50.02 ? 330 LYS A NZ  1 
ATOM   2641 N N   . GLU A 1 330 ? 13.279  -28.713 21.049  1.00 31.65 ? 331 GLU A N   1 
ATOM   2642 C CA  . GLU A 1 330 ? 12.682  -27.510 21.611  1.00 33.03 ? 331 GLU A CA  1 
ATOM   2643 C C   . GLU A 1 330 ? 11.580  -26.931 20.731  1.00 30.04 ? 331 GLU A C   1 
ATOM   2644 O O   . GLU A 1 330 ? 11.010  -25.887 21.076  1.00 29.75 ? 331 GLU A O   1 
ATOM   2645 C CB  . GLU A 1 330 ? 13.771  -26.463 21.852  1.00 34.20 ? 331 GLU A CB  1 
ATOM   2646 C CG  . GLU A 1 330 ? 14.862  -26.943 22.813  1.00 36.50 ? 331 GLU A CG  1 
ATOM   2647 C CD  . GLU A 1 330 ? 14.361  -27.086 24.237  1.00 45.41 ? 331 GLU A CD  1 
ATOM   2648 O OE1 . GLU A 1 330 ? 14.515  -26.126 25.018  1.00 53.24 ? 331 GLU A OE1 1 
ATOM   2649 O OE2 . GLU A 1 330 ? 13.805  -28.151 24.579  1.00 47.22 ? 331 GLU A OE2 1 
ATOM   2650 N N   . ASN A 1 331 ? 11.268  -27.595 19.615  1.00 25.66 ? 332 ASN A N   1 
ATOM   2651 C CA  . ASN A 1 331 ? 10.230  -27.164 18.681  1.00 25.58 ? 332 ASN A CA  1 
ATOM   2652 C C   . ASN A 1 331 ? 10.381  -25.694 18.318  1.00 24.43 ? 332 ASN A C   1 
ATOM   2653 O O   . ASN A 1 331 ? 9.409   -24.932 18.308  1.00 26.13 ? 332 ASN A O   1 
ATOM   2654 C CB  . ASN A 1 331 ? 8.841   -27.437 19.239  1.00 30.95 ? 332 ASN A CB  1 
ATOM   2655 C CG  . ASN A 1 331 ? 8.373   -28.809 18.910  1.00 40.58 ? 332 ASN A CG  1 
ATOM   2656 O OD1 . ASN A 1 331 ? 8.270   -29.662 19.785  1.00 41.54 ? 332 ASN A OD1 1 
ATOM   2657 N ND2 . ASN A 1 331 ? 8.115   -29.053 17.621  1.00 42.68 ? 332 ASN A ND2 1 
ATOM   2658 N N   . ILE A 1 332 ? 11.613  -25.286 18.029  1.00 22.48 ? 333 ILE A N   1 
ATOM   2659 C CA  . ILE A 1 332 ? 11.903  -23.877 17.813  1.00 21.95 ? 333 ILE A CA  1 
ATOM   2660 C C   . ILE A 1 332 ? 12.946  -23.725 16.711  1.00 21.75 ? 333 ILE A C   1 
ATOM   2661 O O   . ILE A 1 332 ? 13.778  -24.607 16.481  1.00 21.13 ? 333 ILE A O   1 
ATOM   2662 C CB  . ILE A 1 332 ? 12.369  -23.203 19.129  1.00 23.81 ? 333 ILE A CB  1 
ATOM   2663 C CG1 . ILE A 1 332 ? 12.255  -21.678 19.037  1.00 25.96 ? 333 ILE A CG1 1 
ATOM   2664 C CG2 . ILE A 1 332 ? 13.795  -23.608 19.468  1.00 25.09 ? 333 ILE A CG2 1 
ATOM   2665 C CD1 . ILE A 1 332 ? 12.433  -20.966 20.384  1.00 26.59 ? 333 ILE A CD1 1 
ATOM   2666 N N   . GLY A 1 333 ? 12.891  -22.589 16.025  1.00 21.07 ? 334 GLY A N   1 
ATOM   2667 C CA  . GLY A 1 333 ? 13.875  -22.279 15.009  1.00 20.84 ? 334 GLY A CA  1 
ATOM   2668 C C   . GLY A 1 333 ? 13.896  -20.789 14.762  1.00 19.94 ? 334 GLY A C   1 
ATOM   2669 O O   . GLY A 1 333 ? 12.997  -20.054 15.180  1.00 20.09 ? 334 GLY A O   1 
ATOM   2670 N N   . LEU A 1 334 ? 14.930  -20.347 14.046  1.00 19.72 ? 335 LEU A N   1 
ATOM   2671 C CA  . LEU A 1 334 ? 15.130  -18.922 13.798  1.00 19.74 ? 335 LEU A CA  1 
ATOM   2672 C C   . LEU A 1 334 ? 15.667  -18.691 12.390  1.00 19.51 ? 335 LEU A C   1 
ATOM   2673 O O   . LEU A 1 334 ? 16.463  -19.483 11.892  1.00 19.46 ? 335 LEU A O   1 
ATOM   2674 C CB  . LEU A 1 334 ? 16.099  -18.336 14.832  1.00 20.20 ? 335 LEU A CB  1 
ATOM   2675 C CG  . LEU A 1 334 ? 16.403  -16.830 14.771  1.00 20.46 ? 335 LEU A CG  1 
ATOM   2676 C CD1 . LEU A 1 334 ? 16.676  -16.310 16.168  1.00 21.55 ? 335 LEU A CD1 1 
ATOM   2677 C CD2 . LEU A 1 334 ? 17.608  -16.565 13.873  1.00 21.85 ? 335 LEU A CD2 1 
ATOM   2678 N N   . VAL A 1 335 ? 15.251  -17.583 11.760  1.00 19.52 ? 336 VAL A N   1 
ATOM   2679 C CA  . VAL A 1 335 ? 15.712  -17.201 10.424  1.00 22.54 ? 336 VAL A CA  1 
ATOM   2680 C C   . VAL A 1 335 ? 16.127  -15.738 10.466  1.00 20.72 ? 336 VAL A C   1 
ATOM   2681 O O   . VAL A 1 335 ? 15.392  -14.907 11.013  1.00 20.75 ? 336 VAL A O   1 
ATOM   2682 C CB  . VAL A 1 335 ? 14.623  -17.391 9.350   1.00 22.33 ? 336 VAL A CB  1 
ATOM   2683 C CG1 . VAL A 1 335 ? 15.077  -16.780 8.020   1.00 21.96 ? 336 VAL A CG1 1 
ATOM   2684 C CG2 . VAL A 1 335 ? 14.258  -18.868 9.190   1.00 20.93 ? 336 VAL A CG2 1 
ATOM   2685 N N   . MET A 1 336 ? 17.305  -15.430 9.907   1.00 20.46 ? 337 MET A N   1 
ATOM   2686 C CA  . MET A 1 336 ? 17.763  -14.049 9.721   1.00 21.28 ? 337 MET A CA  1 
ATOM   2687 C C   . MET A 1 336 ? 18.043  -13.821 8.245   1.00 22.46 ? 337 MET A C   1 
ATOM   2688 O O   . MET A 1 336 ? 18.782  -14.598 7.630   1.00 21.58 ? 337 MET A O   1 
ATOM   2689 C CB  . MET A 1 336 ? 19.042  -13.746 10.533  1.00 21.53 ? 337 MET A CB  1 
ATOM   2690 C CG  . MET A 1 336 ? 19.528  -12.277 10.442  1.00 25.94 ? 337 MET A CG  1 
ATOM   2691 S SD  . MET A 1 336 ? 21.294  -12.088 10.812  1.00 32.39 ? 337 MET A SD  1 
ATOM   2692 C CE  . MET A 1 336 ? 21.958  -11.785 9.179   1.00 38.18 ? 337 MET A CE  1 
ATOM   2693 N N   . LEU A 1 337 ? 17.474  -12.750 7.684   1.00 21.63 ? 338 LEU A N   1 
ATOM   2694 C CA  . LEU A 1 337 ? 17.721  -12.344 6.307   1.00 22.19 ? 338 LEU A CA  1 
ATOM   2695 C C   . LEU A 1 337 ? 18.134  -10.879 6.314   1.00 24.94 ? 338 LEU A C   1 
ATOM   2696 O O   . LEU A 1 337 ? 17.505  -10.078 7.005   1.00 23.55 ? 338 LEU A O   1 
ATOM   2697 C CB  . LEU A 1 337 ? 16.462  -12.525 5.446   1.00 23.72 ? 338 LEU A CB  1 
ATOM   2698 C CG  . LEU A 1 337 ? 15.711  -13.863 5.533   1.00 24.43 ? 338 LEU A CG  1 
ATOM   2699 C CD1 . LEU A 1 337 ? 14.371  -13.801 4.797   1.00 23.39 ? 338 LEU A CD1 1 
ATOM   2700 C CD2 . LEU A 1 337 ? 16.559  -14.974 4.965   1.00 22.74 ? 338 LEU A CD2 1 
ATOM   2701 N N   . THR A 1 338 ? 19.204  -10.529 5.590   1.00 25.76 ? 339 THR A N   1 
ATOM   2702 C CA  . THR A 1 338 ? 19.575  -9.123  5.401   1.00 25.20 ? 339 THR A CA  1 
ATOM   2703 C C   . THR A 1 338 ? 19.951  -8.894  3.944   1.00 28.19 ? 339 THR A C   1 
ATOM   2704 O O   . THR A 1 338 ? 20.149  -9.840  3.174   1.00 27.73 ? 339 THR A O   1 
ATOM   2705 C CB  . THR A 1 338 ? 20.744  -8.686  6.303   1.00 31.38 ? 339 THR A CB  1 
ATOM   2706 O OG1 . THR A 1 338 ? 21.918  -9.437  5.967   1.00 34.83 ? 339 THR A OG1 1 
ATOM   2707 C CG2 . THR A 1 338 ? 20.420  -8.885  7.783   1.00 29.30 ? 339 THR A CG2 1 
ATOM   2708 N N   . ASN A 1 339 ? 20.039  -7.613  3.556   1.00 27.31 ? 340 ASN A N   1 
ATOM   2709 C CA  . ASN A 1 339 ? 20.488  -7.241  2.220   1.00 31.56 ? 340 ASN A CA  1 
ATOM   2710 C C   . ASN A 1 339 ? 21.899  -6.649  2.237   1.00 35.31 ? 340 ASN A C   1 
ATOM   2711 O O   . ASN A 1 339 ? 22.260  -5.852  1.366   1.00 34.29 ? 340 ASN A O   1 
ATOM   2712 C CB  . ASN A 1 339 ? 19.498  -6.282  1.550   1.00 32.28 ? 340 ASN A CB  1 
ATOM   2713 C CG  . ASN A 1 339 ? 19.216  -5.044  2.380   1.00 30.23 ? 340 ASN A CG  1 
ATOM   2714 O OD1 . ASN A 1 339 ? 19.795  -4.848  3.449   1.00 30.53 ? 340 ASN A OD1 1 
ATOM   2715 N ND2 . ASN A 1 339 ? 18.324  -4.184  1.877   1.00 32.18 ? 340 ASN A ND2 1 
ATOM   2716 N N   . LYS A 1 340 ? 22.701  -7.032  3.227   1.00 33.36 ? 341 LYS A N   1 
ATOM   2717 C CA  . LYS A 1 340 ? 24.123  -6.713  3.259   1.00 36.35 ? 341 LYS A CA  1 
ATOM   2718 C C   . LYS A 1 340 ? 24.823  -7.747  4.131   1.00 34.53 ? 341 LYS A C   1 
ATOM   2719 O O   . LYS A 1 340 ? 24.251  -8.241  5.101   1.00 35.57 ? 341 LYS A O   1 
ATOM   2720 C CB  . LYS A 1 340 ? 24.396  -5.301  3.791   1.00 33.88 ? 341 LYS A CB  1 
ATOM   2721 C CG  . LYS A 1 340 ? 25.872  -4.906  3.743   1.00 35.20 ? 341 LYS A CG  1 
ATOM   2722 C CD  . LYS A 1 340 ? 26.099  -3.549  4.376   1.00 35.72 ? 341 LYS A CD  1 
ATOM   2723 C CE  . LYS A 1 340 ? 27.543  -3.086  4.234   1.00 45.02 ? 341 LYS A CE  1 
ATOM   2724 N NZ  . LYS A 1 340 ? 27.725  -1.731  4.838   1.00 42.86 ? 341 LYS A NZ  1 
ATOM   2725 N N   . ARG A 1 341 ? 26.063  -8.064  3.768   1.00 39.74 ? 342 ARG A N   1 
ATOM   2726 C CA  . ARG A 1 341 ? 26.857  -9.032  4.518   1.00 41.28 ? 342 ARG A CA  1 
ATOM   2727 C C   . ARG A 1 341 ? 27.038  -8.599  5.969   1.00 35.83 ? 342 ARG A C   1 
ATOM   2728 O O   . ARG A 1 341 ? 27.197  -7.415  6.266   1.00 32.14 ? 342 ARG A O   1 
ATOM   2729 C CB  . ARG A 1 341 ? 28.228  -9.196  3.859   1.00 47.16 ? 342 ARG A CB  1 
ATOM   2730 C CG  . ARG A 1 341 ? 28.626  -10.628 3.598   1.00 55.49 ? 342 ARG A CG  1 
ATOM   2731 C CD  . ARG A 1 341 ? 30.143  -10.757 3.472   1.00 59.59 ? 342 ARG A CD  1 
ATOM   2732 N NE  . ARG A 1 341 ? 30.829  -10.327 4.687   1.00 57.07 ? 342 ARG A NE  1 
ATOM   2733 C CZ  . ARG A 1 341 ? 30.869  -11.022 5.819   1.00 52.76 ? 342 ARG A CZ  1 
ATOM   2734 N NH1 . ARG A 1 341 ? 30.246  -12.188 5.942   1.00 51.32 ? 342 ARG A NH1 1 
ATOM   2735 N NH2 . ARG A 1 341 ? 31.549  -10.535 6.856   1.00 50.73 ? 342 ARG A NH2 1 
ATOM   2736 N N   . ILE A 1 342 ? 27.020  -9.577  6.868   1.00 37.18 ? 343 ILE A N   1 
ATOM   2737 C CA  . ILE A 1 342 ? 27.296  -9.422  8.297   1.00 36.39 ? 343 ILE A CA  1 
ATOM   2738 C C   . ILE A 1 342 ? 28.210  -10.591 8.654   1.00 35.53 ? 343 ILE A C   1 
ATOM   2739 O O   . ILE A 1 342 ? 27.952  -11.703 8.182   1.00 35.32 ? 343 ILE A O   1 
ATOM   2740 C CB  . ILE A 1 342 ? 25.996  -9.449  9.124   1.00 35.54 ? 343 ILE A CB  1 
ATOM   2741 C CG1 . ILE A 1 342 ? 25.131  -8.218  8.857   1.00 39.67 ? 343 ILE A CG1 1 
ATOM   2742 C CG2 . ILE A 1 342 ? 26.270  -9.559  10.611  1.00 38.19 ? 343 ILE A CG2 1 
ATOM   2743 C CD1 . ILE A 1 342 ? 23.827  -8.235  9.662   1.00 34.39 ? 343 ILE A CD1 1 
ATOM   2744 N N   . PRO A 1 343 ? 29.268  -10.414 9.445   1.00 33.57 ? 344 PRO A N   1 
ATOM   2745 C CA  . PRO A 1 343 ? 30.135  -11.556 9.782   1.00 37.43 ? 344 PRO A CA  1 
ATOM   2746 C C   . PRO A 1 343 ? 29.339  -12.726 10.351  1.00 37.00 ? 344 PRO A C   1 
ATOM   2747 O O   . PRO A 1 343 ? 28.490  -12.553 11.229  1.00 34.36 ? 344 PRO A O   1 
ATOM   2748 C CB  . PRO A 1 343 ? 31.105  -10.973 10.817  1.00 39.03 ? 344 PRO A CB  1 
ATOM   2749 C CG  . PRO A 1 343 ? 31.147  -9.503  10.516  1.00 37.95 ? 344 PRO A CG  1 
ATOM   2750 C CD  . PRO A 1 343 ? 29.749  -9.154  10.044  1.00 34.11 ? 344 PRO A CD  1 
ATOM   2751 N N   . ASN A 1 344 ? 29.591  -13.922 9.807   1.00 37.41 ? 345 ASN A N   1 
ATOM   2752 C CA  . ASN A 1 344 ? 28.903  -15.124 10.281  1.00 37.20 ? 345 ASN A CA  1 
ATOM   2753 C C   . ASN A 1 344 ? 28.965  -15.238 11.799  1.00 34.45 ? 345 ASN A C   1 
ATOM   2754 O O   . ASN A 1 344 ? 27.970  -15.589 12.447  1.00 32.24 ? 345 ASN A O   1 
ATOM   2755 C CB  . ASN A 1 344 ? 29.513  -16.370 9.638   1.00 39.00 ? 345 ASN A CB  1 
ATOM   2756 C CG  . ASN A 1 344 ? 28.980  -16.627 8.248   1.00 46.81 ? 345 ASN A CG  1 
ATOM   2757 O OD1 . ASN A 1 344 ? 27.779  -16.501 7.996   1.00 45.32 ? 345 ASN A OD1 1 
ATOM   2758 N ND2 . ASN A 1 344 ? 29.871  -16.998 7.334   1.00 49.11 ? 345 ASN A ND2 1 
ATOM   2759 N N   . GLU A 1 345 ? 30.130  -14.935 12.376  1.00 31.98 ? 346 GLU A N   1 
ATOM   2760 C CA  . GLU A 1 345 ? 30.287  -14.925 13.825  1.00 33.59 ? 346 GLU A CA  1 
ATOM   2761 C C   . GLU A 1 345 ? 29.160  -14.156 14.502  1.00 34.90 ? 346 GLU A C   1 
ATOM   2762 O O   . GLU A 1 345 ? 28.592  -14.621 15.497  1.00 31.97 ? 346 GLU A O   1 
ATOM   2763 C CB  . GLU A 1 345 ? 31.660  -14.329 14.176  1.00 39.28 ? 346 GLU A CB  1 
ATOM   2764 C CG  . GLU A 1 345 ? 31.777  -13.694 15.557  1.00 40.30 ? 346 GLU A CG  1 
ATOM   2765 C CD  . GLU A 1 345 ? 31.480  -12.202 15.554  1.00 48.61 ? 346 GLU A CD  1 
ATOM   2766 O OE1 . GLU A 1 345 ? 32.127  -11.452 14.780  1.00 53.23 ? 346 GLU A OE1 1 
ATOM   2767 O OE2 . GLU A 1 345 ? 30.586  -11.776 16.324  1.00 49.25 ? 346 GLU A OE2 1 
ATOM   2768 N N   . GLU A 1 346 ? 28.810  -12.980 13.965  1.00 32.78 ? 347 GLU A N   1 
ATOM   2769 C CA  . GLU A 1 346 ? 27.780  -12.161 14.590  1.00 32.39 ? 347 GLU A CA  1 
ATOM   2770 C C   . GLU A 1 346 ? 26.399  -12.780 14.446  1.00 29.44 ? 347 GLU A C   1 
ATOM   2771 O O   . GLU A 1 346 ? 25.567  -12.638 15.347  1.00 28.39 ? 347 GLU A O   1 
ATOM   2772 C CB  . GLU A 1 346 ? 27.791  -10.751 13.990  1.00 37.39 ? 347 GLU A CB  1 
ATOM   2773 C CG  . GLU A 1 346 ? 29.063  -9.963  14.254  1.00 39.91 ? 347 GLU A CG  1 
ATOM   2774 C CD  . GLU A 1 346 ? 29.019  -9.177  15.560  1.00 43.12 ? 347 GLU A CD  1 
ATOM   2775 O OE1 . GLU A 1 346 ? 29.664  -8.103  15.643  1.00 40.88 ? 347 GLU A OE1 1 
ATOM   2776 O OE2 . GLU A 1 346 ? 28.333  -9.632  16.499  1.00 42.24 ? 347 GLU A OE2 1 
ATOM   2777 N N   . ARG A 1 347 ? 26.126  -13.446 13.320  1.00 28.39 ? 348 ARG A N   1 
ATOM   2778 C CA  . ARG A 1 347 ? 24.824  -14.080 13.142  1.00 29.62 ? 348 ARG A CA  1 
ATOM   2779 C C   . ARG A 1 347 ? 24.645  -15.213 14.141  1.00 27.44 ? 348 ARG A C   1 
ATOM   2780 O O   . ARG A 1 347 ? 23.581  -15.351 14.756  1.00 27.46 ? 348 ARG A O   1 
ATOM   2781 C CB  . ARG A 1 347 ? 24.675  -14.621 11.717  1.00 28.85 ? 348 ARG A CB  1 
ATOM   2782 C CG  . ARG A 1 347 ? 25.084  -13.668 10.590  1.00 32.89 ? 348 ARG A CG  1 
ATOM   2783 C CD  . ARG A 1 347 ? 25.000  -14.363 9.212   1.00 33.67 ? 348 ARG A CD  1 
ATOM   2784 N NE  . ARG A 1 347 ? 25.889  -13.745 8.230   1.00 39.27 ? 348 ARG A NE  1 
ATOM   2785 C CZ  . ARG A 1 347 ? 26.113  -14.201 7.002   1.00 42.77 ? 348 ARG A CZ  1 
ATOM   2786 N NH1 . ARG A 1 347 ? 25.496  -15.272 6.535   1.00 37.01 ? 348 ARG A NH1 1 
ATOM   2787 N NH2 . ARG A 1 347 ? 26.988  -13.566 6.222   1.00 44.79 ? 348 ARG A NH2 1 
ATOM   2788 N N   . ILE A 1 348 ? 25.684  -16.031 14.302  1.00 30.19 ? 349 ILE A N   1 
ATOM   2789 C CA  . ILE A 1 348 ? 25.616  -17.179 15.200  1.00 28.66 ? 349 ILE A CA  1 
ATOM   2790 C C   . ILE A 1 348 ? 25.449  -16.717 16.647  1.00 28.13 ? 349 ILE A C   1 
ATOM   2791 O O   . ILE A 1 348 ? 24.606  -17.240 17.387  1.00 29.13 ? 349 ILE A O   1 
ATOM   2792 C CB  . ILE A 1 348 ? 26.864  -18.062 15.013  1.00 29.43 ? 349 ILE A CB  1 
ATOM   2793 C CG1 . ILE A 1 348 ? 26.916  -18.612 13.583  1.00 26.51 ? 349 ILE A CG1 1 
ATOM   2794 C CG2 . ILE A 1 348 ? 26.875  -19.209 16.023  1.00 29.77 ? 349 ILE A CG2 1 
ATOM   2795 C CD1 . ILE A 1 348 ? 28.231  -19.309 13.241  1.00 30.68 ? 349 ILE A CD1 1 
ATOM   2796 N N   . LYS A 1 349 ? 26.226  -15.713 17.062  1.00 28.46 ? 350 LYS A N   1 
ATOM   2797 C CA  . LYS A 1 349 ? 26.145  -15.227 18.438  1.00 30.14 ? 350 LYS A CA  1 
ATOM   2798 C C   . LYS A 1 349 ? 24.767  -14.663 18.751  1.00 31.07 ? 350 LYS A C   1 
ATOM   2799 O O   . LYS A 1 349 ? 24.196  -14.951 19.809  1.00 27.76 ? 350 LYS A O   1 
ATOM   2800 C CB  . LYS A 1 349 ? 27.207  -14.165 18.693  1.00 30.77 ? 350 LYS A CB  1 
ATOM   2801 C CG  . LYS A 1 349 ? 28.601  -14.710 18.924  1.00 35.75 ? 350 LYS A CG  1 
ATOM   2802 C CD  . LYS A 1 349 ? 29.581  -13.572 19.207  1.00 36.98 ? 350 LYS A CD  1 
ATOM   2803 C CE  . LYS A 1 349 ? 31.022  -14.071 19.271  1.00 38.17 ? 350 LYS A CE  1 
ATOM   2804 N NZ  . LYS A 1 349 ? 31.989  -12.940 19.380  1.00 48.00 ? 350 LYS A NZ  1 
ATOM   2805 N N   . ALA A 1 350 ? 24.220  -13.848 17.839  1.00 29.10 ? 351 ALA A N   1 
ATOM   2806 C CA  . ALA A 1 350 ? 22.911  -13.244 18.082  1.00 28.52 ? 351 ALA A CA  1 
ATOM   2807 C C   . ALA A 1 350 ? 21.817  -14.302 18.161  1.00 28.10 ? 351 ALA A C   1 
ATOM   2808 O O   . ALA A 1 350 ? 20.933  -14.230 19.027  1.00 26.99 ? 351 ALA A O   1 
ATOM   2809 C CB  . ALA A 1 350 ? 22.597  -12.211 16.992  1.00 25.87 ? 351 ALA A CB  1 
ATOM   2810 N N   . ALA A 1 351 ? 21.842  -15.288 17.255  1.00 27.59 ? 352 ALA A N   1 
ATOM   2811 C CA  . ALA A 1 351 ? 20.835  -16.341 17.303  1.00 24.91 ? 352 ALA A CA  1 
ATOM   2812 C C   . ALA A 1 351 ? 20.990  -17.200 18.550  1.00 24.76 ? 352 ALA A C   1 
ATOM   2813 O O   . ALA A 1 351 ? 19.989  -17.634 19.133  1.00 24.38 ? 352 ALA A O   1 
ATOM   2814 C CB  . ALA A 1 351 ? 20.908  -17.215 16.052  1.00 21.95 ? 352 ALA A CB  1 
ATOM   2815 N N   . TYR A 1 352 ? 22.232  -17.485 18.951  1.00 23.53 ? 353 TYR A N   1 
ATOM   2816 C CA  . TYR A 1 352 ? 22.459  -18.259 20.170  1.00 25.21 ? 353 TYR A CA  1 
ATOM   2817 C C   . TYR A 1 352 ? 21.848  -17.565 21.378  1.00 25.52 ? 353 TYR A C   1 
ATOM   2818 O O   . TYR A 1 352 ? 21.211  -18.205 22.223  1.00 24.92 ? 353 TYR A O   1 
ATOM   2819 C CB  . TYR A 1 352 ? 23.961  -18.474 20.378  1.00 25.23 ? 353 TYR A CB  1 
ATOM   2820 C CG  . TYR A 1 352 ? 24.326  -19.309 21.599  1.00 25.51 ? 353 TYR A CG  1 
ATOM   2821 C CD1 . TYR A 1 352 ? 24.537  -18.719 22.846  1.00 26.49 ? 353 TYR A CD1 1 
ATOM   2822 C CD2 . TYR A 1 352 ? 24.467  -20.687 21.501  1.00 28.44 ? 353 TYR A CD2 1 
ATOM   2823 C CE1 . TYR A 1 352 ? 24.873  -19.490 23.961  1.00 30.10 ? 353 TYR A CE1 1 
ATOM   2824 C CE2 . TYR A 1 352 ? 24.800  -21.461 22.607  1.00 28.25 ? 353 TYR A CE2 1 
ATOM   2825 C CZ  . TYR A 1 352 ? 25.003  -20.866 23.827  1.00 29.90 ? 353 TYR A CZ  1 
ATOM   2826 O OH  . TYR A 1 352 ? 25.326  -21.654 24.918  1.00 28.13 ? 353 TYR A OH  1 
ATOM   2827 N N   . ALA A 1 353 ? 22.021  -16.248 21.472  1.00 25.52 ? 354 ALA A N   1 
ATOM   2828 C CA  . ALA A 1 353 ? 21.523  -15.541 22.643  1.00 26.88 ? 354 ALA A CA  1 
ATOM   2829 C C   . ALA A 1 353 ? 20.001  -15.517 22.658  1.00 28.67 ? 354 ALA A C   1 
ATOM   2830 O O   . ALA A 1 353 ? 19.384  -15.680 23.717  1.00 28.51 ? 354 ALA A O   1 
ATOM   2831 C CB  . ALA A 1 353 ? 22.095  -14.124 22.691  1.00 26.47 ? 354 ALA A CB  1 
ATOM   2832 N N   . VAL A 1 354 ? 19.379  -15.337 21.491  1.00 25.28 ? 355 VAL A N   1 
ATOM   2833 C CA  . VAL A 1 354 ? 17.922  -15.329 21.424  1.00 24.46 ? 355 VAL A CA  1 
ATOM   2834 C C   . VAL A 1 354 ? 17.370  -16.704 21.772  1.00 29.29 ? 355 VAL A C   1 
ATOM   2835 O O   . VAL A 1 354 ? 16.465  -16.837 22.603  1.00 30.15 ? 355 VAL A O   1 
ATOM   2836 C CB  . VAL A 1 354 ? 17.455  -14.874 20.031  1.00 26.61 ? 355 VAL A CB  1 
ATOM   2837 C CG1 . VAL A 1 354 ? 15.950  -15.100 19.874  1.00 29.58 ? 355 VAL A CG1 1 
ATOM   2838 C CG2 . VAL A 1 354 ? 17.823  -13.417 19.800  1.00 26.96 ? 355 VAL A CG2 1 
ATOM   2839 N N   . LEU A 1 355 ? 17.907  -17.751 21.146  1.00 25.47 ? 356 LEU A N   1 
ATOM   2840 C CA  . LEU A 1 355 ? 17.341  -19.079 21.364  1.00 26.99 ? 356 LEU A CA  1 
ATOM   2841 C C   . LEU A 1 355 ? 17.568  -19.570 22.788  1.00 28.33 ? 356 LEU A C   1 
ATOM   2842 O O   . LEU A 1 355 ? 16.722  -20.282 23.337  1.00 30.88 ? 356 LEU A O   1 
ATOM   2843 C CB  . LEU A 1 355 ? 17.920  -20.070 20.360  1.00 28.89 ? 356 LEU A CB  1 
ATOM   2844 C CG  . LEU A 1 355 ? 17.470  -19.811 18.925  1.00 31.69 ? 356 LEU A CG  1 
ATOM   2845 C CD1 . LEU A 1 355 ? 18.121  -20.830 18.019  1.00 33.78 ? 356 LEU A CD1 1 
ATOM   2846 C CD2 . LEU A 1 355 ? 15.950  -19.878 18.808  1.00 29.57 ? 356 LEU A CD2 1 
ATOM   2847 N N   . ASN A 1 356 ? 18.696  -19.213 23.400  1.00 25.93 ? 357 ASN A N   1 
ATOM   2848 C CA  . ASN A 1 356 ? 18.944  -19.627 24.772  1.00 26.41 ? 357 ASN A CA  1 
ATOM   2849 C C   . ASN A 1 356 ? 18.060  -18.896 25.777  1.00 30.62 ? 357 ASN A C   1 
ATOM   2850 O O   . ASN A 1 356 ? 17.947  -19.343 26.922  1.00 32.89 ? 357 ASN A O   1 
ATOM   2851 C CB  . ASN A 1 356 ? 20.414  -19.409 25.127  1.00 26.81 ? 357 ASN A CB  1 
ATOM   2852 C CG  . ASN A 1 356 ? 21.276  -20.591 24.768  1.00 28.39 ? 357 ASN A CG  1 
ATOM   2853 O OD1 . ASN A 1 356 ? 21.647  -21.389 25.637  1.00 32.43 ? 357 ASN A OD1 1 
ATOM   2854 N ND2 . ASN A 1 356 ? 21.594  -20.728 23.488  1.00 28.52 ? 357 ASN A ND2 1 
ATOM   2855 N N   . ALA A 1 357 ? 17.439  -17.785 25.392  1.00 29.55 ? 358 ALA A N   1 
ATOM   2856 C CA  . ALA A 1 357 ? 16.638  -17.025 26.342  1.00 33.22 ? 358 ALA A CA  1 
ATOM   2857 C C   . ALA A 1 357 ? 15.141  -17.256 26.196  1.00 40.30 ? 358 ALA A C   1 
ATOM   2858 O O   . ALA A 1 357 ? 14.384  -16.900 27.105  1.00 39.93 ? 358 ALA A O   1 
ATOM   2859 C CB  . ALA A 1 357 ? 16.929  -15.525 26.203  1.00 31.60 ? 358 ALA A CB  1 
ATOM   2860 N N   . ILE A 1 358 ? 14.691  -17.831 25.084  1.00 37.02 ? 359 ILE A N   1 
ATOM   2861 C CA  . ILE A 1 358 ? 13.258  -17.945 24.859  1.00 41.35 ? 359 ILE A CA  1 
ATOM   2862 C C   . ILE A 1 358 ? 12.686  -18.975 25.822  1.00 49.62 ? 359 ILE A C   1 
ATOM   2863 O O   . ILE A 1 358 ? 13.153  -20.120 25.880  1.00 52.24 ? 359 ILE A O   1 
ATOM   2864 C CB  . ILE A 1 358 ? 12.952  -18.298 23.401  1.00 38.79 ? 359 ILE A CB  1 
ATOM   2865 C CG1 . ILE A 1 358 ? 13.248  -17.090 22.512  1.00 40.50 ? 359 ILE A CG1 1 
ATOM   2866 C CG2 . ILE A 1 358 ? 11.502  -18.725 23.254  1.00 44.77 ? 359 ILE A CG2 1 
ATOM   2867 C CD1 . ILE A 1 358 ? 12.633  -17.170 21.149  1.00 35.13 ? 359 ILE A CD1 1 
ATOM   2868 N N   . LYS A 1 359 ? 11.688  -18.558 26.599  1.00 54.85 ? 360 LYS A N   1 
ATOM   2869 C CA  . LYS A 1 359 ? 11.001  -19.470 27.499  1.00 59.40 ? 360 LYS A CA  1 
ATOM   2870 C C   . LYS A 1 359 ? 10.198  -20.480 26.692  1.00 63.36 ? 360 LYS A C   1 
ATOM   2871 O O   . LYS A 1 359 ? 9.645   -20.156 25.636  1.00 57.69 ? 360 LYS A O   1 
ATOM   2872 C CB  . LYS A 1 359 ? 10.077  -18.695 28.440  1.00 62.37 ? 360 LYS A CB  1 
ATOM   2873 C CG  . LYS A 1 359 ? 10.701  -17.453 29.074  1.00 65.61 ? 360 LYS A CG  1 
ATOM   2874 C CD  . LYS A 1 359 ? 9.735   -16.814 30.074  1.00 73.30 ? 360 LYS A CD  1 
ATOM   2875 C CE  . LYS A 1 359 ? 10.321  -15.577 30.745  1.00 70.42 ? 360 LYS A CE  1 
ATOM   2876 N NZ  . LYS A 1 359 ? 10.433  -14.432 29.802  1.00 68.23 ? 360 LYS A NZ  1 
ATOM   2877 N N   . LYS A 1 360 ? 10.135  -21.709 27.194  1.00 72.46 ? 361 LYS A N   1 
ATOM   2878 C CA  . LYS A 1 360 ? 9.432   -22.790 26.509  1.00 73.73 ? 361 LYS A CA  1 
ATOM   2879 C C   . LYS A 1 360 ? 7.924   -22.519 26.400  1.00 73.28 ? 361 LYS A C   1 
ATOM   2880 O O   . LYS A 1 360 ? 7.168   -23.353 25.899  1.00 70.97 ? 361 LYS A O   1 
ATOM   2881 C CB  . LYS A 1 360 ? 9.676   -24.117 27.233  1.00 72.33 ? 361 LYS A CB  1 
ATOM   2882 C CG  . LYS A 1 360 ? 10.991  -24.178 28.016  1.00 73.47 ? 361 LYS A CG  1 
ATOM   2883 C CD  . LYS A 1 360 ? 12.214  -24.289 27.108  1.00 67.55 ? 361 LYS A CD  1 
ATOM   2884 C CE  . LYS A 1 360 ? 13.501  -24.417 27.926  1.00 63.21 ? 361 LYS A CE  1 
ATOM   2885 N NZ  . LYS A 1 360 ? 13.463  -25.557 28.888  1.00 57.48 ? 361 LYS A NZ  1 
ATOM   2886 O OXT . LYS A 1 360 ? 7.412   -21.470 26.803  1.00 71.33 ? 361 LYS A OXT 1 
ATOM   2887 N N   . ASN B 1 2   ? -4.964  -3.502  -8.024  1.00 75.80 ? 3   ASN B N   1 
ATOM   2888 C CA  . ASN B 1 2   ? -4.858  -2.047  -8.036  1.00 74.39 ? 3   ASN B CA  1 
ATOM   2889 C C   . ASN B 1 2   ? -5.266  -1.468  -9.384  1.00 72.87 ? 3   ASN B C   1 
ATOM   2890 O O   . ASN B 1 2   ? -4.563  -1.631  -10.382 1.00 73.18 ? 3   ASN B O   1 
ATOM   2891 C CB  . ASN B 1 2   ? -3.437  -1.616  -7.684  1.00 74.97 ? 3   ASN B CB  1 
ATOM   2892 C CG  . ASN B 1 2   ? -3.169  -1.672  -6.197  1.00 81.25 ? 3   ASN B CG  1 
ATOM   2893 O OD1 . ASN B 1 2   ? -3.887  -1.061  -5.401  1.00 80.80 ? 3   ASN B OD1 1 
ATOM   2894 N ND2 . ASN B 1 2   ? -2.140  -2.419  -5.808  1.00 85.53 ? 3   ASN B ND2 1 
ATOM   2895 N N   . THR B 1 3   ? -6.408  -0.781  -9.391  1.00 71.29 ? 4   THR B N   1 
ATOM   2896 C CA  . THR B 1 3   ? -7.023  -0.192  -10.575 1.00 74.82 ? 4   THR B CA  1 
ATOM   2897 C C   . THR B 1 3   ? -6.053  0.715   -11.331 1.00 75.16 ? 4   THR B C   1 
ATOM   2898 O O   . THR B 1 3   ? -5.039  1.150   -10.766 1.00 70.69 ? 4   THR B O   1 
ATOM   2899 C CB  . THR B 1 3   ? -8.277  0.591   -10.168 1.00 74.60 ? 4   THR B CB  1 
ATOM   2900 O OG1 . THR B 1 3   ? -7.914  1.659   -9.280  1.00 69.83 ? 4   THR B OG1 1 
ATOM   2901 C CG2 . THR B 1 3   ? -9.271  -0.327  -9.473  1.00 73.06 ? 4   THR B CG2 1 
ATOM   2902 N N   . PRO B 1 4   ? -6.319  1.016   -12.608 1.00 78.30 ? 5   PRO B N   1 
ATOM   2903 C CA  . PRO B 1 4   ? -5.443  1.956   -13.332 1.00 76.37 ? 5   PRO B CA  1 
ATOM   2904 C C   . PRO B 1 4   ? -5.362  3.331   -12.687 1.00 71.93 ? 5   PRO B C   1 
ATOM   2905 O O   . PRO B 1 4   ? -4.358  4.035   -12.863 1.00 67.55 ? 5   PRO B O   1 
ATOM   2906 C CB  . PRO B 1 4   ? -6.085  2.029   -14.726 1.00 84.40 ? 5   PRO B CB  1 
ATOM   2907 C CG  . PRO B 1 4   ? -6.855  0.756   -14.860 1.00 81.57 ? 5   PRO B CG  1 
ATOM   2908 C CD  . PRO B 1 4   ? -7.351  0.431   -13.485 1.00 79.16 ? 5   PRO B CD  1 
ATOM   2909 N N   . LYS B 1 5   ? -6.393  3.734   -11.944 1.00 71.58 ? 6   LYS B N   1 
ATOM   2910 C CA  . LYS B 1 5   ? -6.381  5.045   -11.305 1.00 66.99 ? 6   LYS B CA  1 
ATOM   2911 C C   . LYS B 1 5   ? -5.372  5.088   -10.164 1.00 59.72 ? 6   LYS B C   1 
ATOM   2912 O O   . LYS B 1 5   ? -4.560  6.019   -10.075 1.00 55.22 ? 6   LYS B O   1 
ATOM   2913 C CB  . LYS B 1 5   ? -7.783  5.388   -10.802 1.00 65.40 ? 6   LYS B CB  1 
ATOM   2914 C CG  . LYS B 1 5   ? -7.941  6.818   -10.319 1.00 58.73 ? 6   LYS B CG  1 
ATOM   2915 C CD  . LYS B 1 5   ? -7.871  7.810   -11.463 1.00 60.66 ? 6   LYS B CD  1 
ATOM   2916 C CE  . LYS B 1 5   ? -8.331  9.183   -11.002 1.00 53.69 ? 6   LYS B CE  1 
ATOM   2917 N NZ  . LYS B 1 5   ? -8.335  10.173  -12.111 1.00 62.38 ? 6   LYS B NZ  1 
ATOM   2918 N N   . ASP B 1 6   ? -5.419  4.090   -9.274  1.00 60.95 ? 7   ASP B N   1 
ATOM   2919 C CA  . ASP B 1 6   ? -4.453  4.005   -8.183  1.00 57.48 ? 7   ASP B CA  1 
ATOM   2920 C C   . ASP B 1 6   ? -3.029  4.021   -8.718  1.00 55.83 ? 7   ASP B C   1 
ATOM   2921 O O   . ASP B 1 6   ? -2.166  4.749   -8.211  1.00 46.05 ? 7   ASP B O   1 
ATOM   2922 C CB  . ASP B 1 6   ? -4.684  2.731   -7.363  1.00 58.99 ? 7   ASP B CB  1 
ATOM   2923 C CG  . ASP B 1 6   ? -5.956  2.779   -6.543  1.00 59.52 ? 7   ASP B CG  1 
ATOM   2924 O OD1 . ASP B 1 6   ? -7.031  2.475   -7.102  1.00 66.42 ? 7   ASP B OD1 1 
ATOM   2925 O OD2 . ASP B 1 6   ? -5.882  3.109   -5.338  1.00 57.45 ? 7   ASP B OD2 1 
ATOM   2926 N N   . GLN B 1 7   ? -2.772  3.220   -9.755  1.00 55.64 ? 8   GLN B N   1 
ATOM   2927 C CA  . GLN B 1 7   ? -1.412  3.076   -10.258 1.00 52.49 ? 8   GLN B CA  1 
ATOM   2928 C C   . GLN B 1 7   ? -0.898  4.382   -10.845 1.00 48.47 ? 8   GLN B C   1 
ATOM   2929 O O   . GLN B 1 7   ? 0.275   4.728   -10.660 1.00 47.69 ? 8   GLN B O   1 
ATOM   2930 C CB  . GLN B 1 7   ? -1.350  1.944   -11.286 1.00 54.59 ? 8   GLN B CB  1 
ATOM   2931 C CG  . GLN B 1 7   ? -1.599  0.567   -10.680 1.00 59.20 ? 8   GLN B CG  1 
ATOM   2932 C CD  . GLN B 1 7   ? -1.391  -0.567  -11.671 1.00 64.78 ? 8   GLN B CD  1 
ATOM   2933 O OE1 . GLN B 1 7   ? -1.091  -0.338  -12.846 1.00 63.81 ? 8   GLN B OE1 1 
ATOM   2934 N NE2 . GLN B 1 7   ? -1.550  -1.804  -11.198 1.00 64.48 ? 8   GLN B NE2 1 
ATOM   2935 N N   . GLU B 1 8   ? -1.758  5.141   -11.529 1.00 47.64 ? 9   GLU B N   1 
ATOM   2936 C CA  . GLU B 1 8   ? -1.286  6.402   -12.091 1.00 49.82 ? 9   GLU B CA  1 
ATOM   2937 C C   . GLU B 1 8   ? -1.046  7.449   -11.005 1.00 41.83 ? 9   GLU B C   1 
ATOM   2938 O O   . GLU B 1 8   ? -0.101  8.240   -11.103 1.00 39.45 ? 9   GLU B O   1 
ATOM   2939 C CB  . GLU B 1 8   ? -2.261  6.932   -13.144 1.00 51.56 ? 9   GLU B CB  1 
ATOM   2940 C CG  . GLU B 1 8   ? -2.042  8.410   -13.514 1.00 55.65 ? 9   GLU B CG  1 
ATOM   2941 C CD  . GLU B 1 8   ? -0.703  8.713   -14.215 1.00 61.19 ? 9   GLU B CD  1 
ATOM   2942 O OE1 . GLU B 1 8   ? -0.721  9.532   -15.160 1.00 65.80 ? 9   GLU B OE1 1 
ATOM   2943 O OE2 . GLU B 1 8   ? 0.363   8.170   -13.830 1.00 53.56 ? 9   GLU B OE2 1 
ATOM   2944 N N   . ILE B 1 9   ? -1.879  7.473   -9.963  1.00 44.15 ? 10  ILE B N   1 
ATOM   2945 C CA  . ILE B 1 9   ? -1.698  8.469   -8.909  1.00 40.56 ? 10  ILE B CA  1 
ATOM   2946 C C   . ILE B 1 9   ? -0.485  8.126   -8.053  1.00 40.31 ? 10  ILE B C   1 
ATOM   2947 O O   . ILE B 1 9   ? 0.266   9.017   -7.631  1.00 36.21 ? 10  ILE B O   1 
ATOM   2948 C CB  . ILE B 1 9   ? -2.979  8.602   -8.064  1.00 39.94 ? 10  ILE B CB  1 
ATOM   2949 C CG1 . ILE B 1 9   ? -4.136  9.077   -8.942  1.00 40.60 ? 10  ILE B CG1 1 
ATOM   2950 C CG2 . ILE B 1 9   ? -2.772  9.562   -6.888  1.00 37.48 ? 10  ILE B CG2 1 
ATOM   2951 C CD1 . ILE B 1 9   ? -5.390  9.411   -8.174  1.00 47.14 ? 10  ILE B CD1 1 
ATOM   2952 N N   . LYS B 1 10  ? -0.272  6.832   -7.780  1.00 38.00 ? 11  LYS B N   1 
ATOM   2953 C CA  . LYS B 1 10  ? 0.927   6.415   -7.059  1.00 38.68 ? 11  LYS B CA  1 
ATOM   2954 C C   . LYS B 1 10  ? 2.185   6.784   -7.834  1.00 36.60 ? 11  LYS B C   1 
ATOM   2955 O O   . LYS B 1 10  ? 3.201   7.162   -7.240  1.00 34.43 ? 11  LYS B O   1 
ATOM   2956 C CB  . LYS B 1 10  ? 0.889   4.906   -6.782  1.00 42.53 ? 11  LYS B CB  1 
ATOM   2957 C CG  . LYS B 1 10  ? 2.266   4.236   -6.867  1.00 48.47 ? 11  LYS B CG  1 
ATOM   2958 C CD  . LYS B 1 10  ? 2.394   2.989   -5.989  1.00 47.65 ? 11  LYS B CD  1 
ATOM   2959 C CE  . LYS B 1 10  ? 3.870   2.626   -5.767  1.00 50.19 ? 11  LYS B CE  1 
ATOM   2960 N NZ  . LYS B 1 10  ? 4.666   2.615   -7.040  1.00 50.19 ? 11  LYS B NZ  1 
ATOM   2961 N N   . LYS B 1 11  ? 2.130   6.687   -9.167  1.00 35.76 ? 12  LYS B N   1 
ATOM   2962 C CA  . LYS B 1 11  ? 3.278   7.050   -9.991  1.00 36.71 ? 12  LYS B CA  1 
ATOM   2963 C C   . LYS B 1 11  ? 3.565   8.549   -9.933  1.00 35.95 ? 12  LYS B C   1 
ATOM   2964 O O   . LYS B 1 11  ? 4.730   8.959   -9.927  1.00 31.15 ? 12  LYS B O   1 
ATOM   2965 C CB  . LYS B 1 11  ? 3.043   6.615   -11.434 1.00 38.94 ? 12  LYS B CB  1 
ATOM   2966 C CG  . LYS B 1 11  ? 4.252   6.799   -12.336 1.00 43.41 ? 12  LYS B CG  1 
ATOM   2967 C CD  . LYS B 1 11  ? 4.341   5.658   -13.349 1.00 47.19 ? 12  LYS B CD  1 
ATOM   2968 C CE  . LYS B 1 11  ? 5.241   6.019   -14.529 1.00 51.33 ? 12  LYS B CE  1 
ATOM   2969 N NZ  . LYS B 1 11  ? 5.357   4.904   -15.526 1.00 56.43 ? 12  LYS B NZ  1 
ATOM   2970 N N   . LEU B 1 12  ? 2.522   9.381   -9.911  1.00 32.90 ? 13  LEU B N   1 
ATOM   2971 C CA  . LEU B 1 12  ? 2.738   10.824  -9.814  1.00 35.69 ? 13  LEU B CA  1 
ATOM   2972 C C   . LEU B 1 12  ? 3.369   11.204  -8.483  1.00 34.50 ? 13  LEU B C   1 
ATOM   2973 O O   . LEU B 1 12  ? 4.273   12.046  -8.437  1.00 32.07 ? 13  LEU B O   1 
ATOM   2974 C CB  . LEU B 1 12  ? 1.422   11.575  -9.998  1.00 36.21 ? 13  LEU B CB  1 
ATOM   2975 C CG  . LEU B 1 12  ? 0.924   11.642  -11.433 1.00 41.48 ? 13  LEU B CG  1 
ATOM   2976 C CD1 . LEU B 1 12  ? -0.400  12.362  -11.487 1.00 39.05 ? 13  LEU B CD1 1 
ATOM   2977 C CD2 . LEU B 1 12  ? 1.964   12.352  -12.277 1.00 43.15 ? 13  LEU B CD2 1 
ATOM   2978 N N   . VAL B 1 13  ? 2.888   10.605  -7.389  1.00 35.05 ? 14  VAL B N   1 
ATOM   2979 C CA  . VAL B 1 13  ? 3.437   10.904  -6.070  1.00 28.84 ? 14  VAL B CA  1 
ATOM   2980 C C   . VAL B 1 13  ? 4.872   10.411  -5.972  1.00 31.58 ? 14  VAL B C   1 
ATOM   2981 O O   . VAL B 1 13  ? 5.747   11.114  -5.453  1.00 32.88 ? 14  VAL B O   1 
ATOM   2982 C CB  . VAL B 1 13  ? 2.537   10.298  -4.975  1.00 30.81 ? 14  VAL B CB  1 
ATOM   2983 C CG1 . VAL B 1 13  ? 3.139   10.525  -3.600  1.00 33.47 ? 14  VAL B CG1 1 
ATOM   2984 C CG2 . VAL B 1 13  ? 1.158   10.916  -5.030  1.00 29.67 ? 14  VAL B CG2 1 
ATOM   2985 N N   . ASP B 1 14  ? 5.136   9.195   -6.474  1.00 30.09 ? 15  ASP B N   1 
ATOM   2986 C CA  . ASP B 1 14  ? 6.495   8.671   -6.549  1.00 34.09 ? 15  ASP B CA  1 
ATOM   2987 C C   . ASP B 1 14  ? 7.410   9.625   -7.293  1.00 33.56 ? 15  ASP B C   1 
ATOM   2988 O O   . ASP B 1 14  ? 8.519   9.926   -6.838  1.00 32.60 ? 15  ASP B O   1 
ATOM   2989 C CB  . ASP B 1 14  ? 6.502   7.315   -7.265  1.00 37.05 ? 15  ASP B CB  1 
ATOM   2990 C CG  . ASP B 1 14  ? 6.376   6.143   -6.321  1.00 37.97 ? 15  ASP B CG  1 
ATOM   2991 O OD1 . ASP B 1 14  ? 6.646   6.310   -5.119  1.00 37.00 ? 15  ASP B OD1 1 
ATOM   2992 O OD2 . ASP B 1 14  ? 6.015   5.045   -6.795  1.00 42.27 ? 15  ASP B OD2 1 
ATOM   2993 N N   . GLN B 1 15  ? 6.973   10.065  -8.478  1.00 33.20 ? 16  GLN B N   1 
ATOM   2994 C CA  . GLN B 1 15  ? 7.797   10.930  -9.320  1.00 32.58 ? 16  GLN B CA  1 
ATOM   2995 C C   . GLN B 1 15  ? 8.199   12.202  -8.594  1.00 32.46 ? 16  GLN B C   1 
ATOM   2996 O O   . GLN B 1 15  ? 9.336   12.668  -8.730  1.00 34.36 ? 16  GLN B O   1 
ATOM   2997 C CB  . GLN B 1 15  ? 7.043   11.306  -10.596 1.00 34.44 ? 16  GLN B CB  1 
ATOM   2998 C CG  . GLN B 1 15  ? 7.067   10.286  -11.716 1.00 42.87 ? 16  GLN B CG  1 
ATOM   2999 C CD  . GLN B 1 15  ? 6.310   10.799  -12.929 1.00 50.42 ? 16  GLN B CD  1 
ATOM   3000 O OE1 . GLN B 1 15  ? 5.077   10.774  -12.963 1.00 49.95 ? 16  GLN B OE1 1 
ATOM   3001 N NE2 . GLN B 1 15  ? 7.043   11.308  -13.914 1.00 55.75 ? 16  GLN B NE2 1 
ATOM   3002 N N   . ASN B 1 16  ? 7.274   12.789  -7.835  1.00 33.22 ? 17  ASN B N   1 
ATOM   3003 C CA  . ASN B 1 16  ? 7.435   14.145  -7.329  1.00 31.24 ? 17  ASN B CA  1 
ATOM   3004 C C   . ASN B 1 16  ? 7.856   14.216  -5.870  1.00 29.18 ? 17  ASN B C   1 
ATOM   3005 O O   . ASN B 1 16  ? 8.486   15.198  -5.473  1.00 32.46 ? 17  ASN B O   1 
ATOM   3006 C CB  . ASN B 1 16  ? 6.133   14.927  -7.517  1.00 27.49 ? 17  ASN B CB  1 
ATOM   3007 C CG  . ASN B 1 16  ? 5.904   15.310  -8.958  1.00 34.22 ? 17  ASN B CG  1 
ATOM   3008 O OD1 . ASN B 1 16  ? 6.484   16.280  -9.443  1.00 31.10 ? 17  ASN B OD1 1 
ATOM   3009 N ND2 . ASN B 1 16  ? 5.062   14.548  -9.658  1.00 29.92 ? 17  ASN B ND2 1 
ATOM   3010 N N   . PHE B 1 17  ? 7.526   13.218  -5.057  1.00 28.99 ? 18  PHE B N   1 
ATOM   3011 C CA  . PHE B 1 17  ? 7.872   13.268  -3.643  1.00 31.59 ? 18  PHE B CA  1 
ATOM   3012 C C   . PHE B 1 17  ? 9.020   12.346  -3.265  1.00 31.34 ? 18  PHE B C   1 
ATOM   3013 O O   . PHE B 1 17  ? 9.818   12.707  -2.399  1.00 31.40 ? 18  PHE B O   1 
ATOM   3014 C CB  . PHE B 1 17  ? 6.647   12.934  -2.778  1.00 26.28 ? 18  PHE B CB  1 
ATOM   3015 C CG  . PHE B 1 17  ? 5.677   14.074  -2.631  1.00 24.67 ? 18  PHE B CG  1 
ATOM   3016 C CD1 . PHE B 1 17  ? 5.812   14.988  -1.597  1.00 24.72 ? 18  PHE B CD1 1 
ATOM   3017 C CD2 . PHE B 1 17  ? 4.633   14.231  -3.526  1.00 27.83 ? 18  PHE B CD2 1 
ATOM   3018 C CE1 . PHE B 1 17  ? 4.937   16.043  -1.455  1.00 24.49 ? 18  PHE B CE1 1 
ATOM   3019 C CE2 . PHE B 1 17  ? 3.743   15.280  -3.402  1.00 28.29 ? 18  PHE B CE2 1 
ATOM   3020 C CZ  . PHE B 1 17  ? 3.893   16.198  -2.357  1.00 27.50 ? 18  PHE B CZ  1 
ATOM   3021 N N   . LYS B 1 18  ? 9.137   11.180  -3.901  1.00 32.01 ? 19  LYS B N   1 
ATOM   3022 C CA  . LYS B 1 18  ? 10.223  10.262  -3.563  1.00 32.99 ? 19  LYS B CA  1 
ATOM   3023 C C   . LYS B 1 18  ? 11.615  10.871  -3.707  1.00 31.74 ? 19  LYS B C   1 
ATOM   3024 O O   . LYS B 1 18  ? 12.455  10.622  -2.825  1.00 34.94 ? 19  LYS B O   1 
ATOM   3025 C CB  . LYS B 1 18  ? 10.099  8.980   -4.401  1.00 36.13 ? 19  LYS B CB  1 
ATOM   3026 C CG  . LYS B 1 18  ? 10.697  7.751   -3.738  1.00 36.79 ? 19  LYS B CG  1 
ATOM   3027 C CD  . LYS B 1 18  ? 10.272  6.475   -4.444  1.00 36.07 ? 19  LYS B CD  1 
ATOM   3028 C CE  . LYS B 1 18  ? 10.934  6.337   -5.800  1.00 41.35 ? 19  LYS B CE  1 
ATOM   3029 N NZ  . LYS B 1 18  ? 10.737  4.958   -6.328  1.00 41.34 ? 19  LYS B NZ  1 
ATOM   3030 N N   . PRO B 1 19  ? 11.938  11.650  -4.745  1.00 33.17 ? 20  PRO B N   1 
ATOM   3031 C CA  . PRO B 1 19  ? 13.287  12.236  -4.799  1.00 33.12 ? 20  PRO B CA  1 
ATOM   3032 C C   . PRO B 1 19  ? 13.548  13.256  -3.701  1.00 34.22 ? 20  PRO B C   1 
ATOM   3033 O O   . PRO B 1 19  ? 14.718  13.549  -3.417  1.00 34.23 ? 20  PRO B O   1 
ATOM   3034 C CB  . PRO B 1 19  ? 13.342  12.880  -6.193  1.00 36.90 ? 20  PRO B CB  1 
ATOM   3035 C CG  . PRO B 1 19  ? 11.929  13.049  -6.602  1.00 36.25 ? 20  PRO B CG  1 
ATOM   3036 C CD  . PRO B 1 19  ? 11.176  11.924  -5.977  1.00 33.68 ? 20  PRO B CD  1 
ATOM   3037 N N   . LEU B 1 20  ? 12.504  13.786  -3.059  1.00 30.97 ? 21  LEU B N   1 
ATOM   3038 C CA  . LEU B 1 20  ? 12.700  14.664  -1.911  1.00 29.37 ? 21  LEU B CA  1 
ATOM   3039 C C   . LEU B 1 20  ? 13.246  13.912  -0.703  1.00 27.30 ? 21  LEU B C   1 
ATOM   3040 O O   . LEU B 1 20  ? 14.032  14.478  0.066   1.00 27.11 ? 21  LEU B O   1 
ATOM   3041 C CB  . LEU B 1 20  ? 11.386  15.360  -1.547  1.00 28.18 ? 21  LEU B CB  1 
ATOM   3042 C CG  . LEU B 1 20  ? 10.842  16.344  -2.577  1.00 28.56 ? 21  LEU B CG  1 
ATOM   3043 C CD1 . LEU B 1 20  ? 9.477   16.861  -2.152  1.00 31.09 ? 21  LEU B CD1 1 
ATOM   3044 C CD2 . LEU B 1 20  ? 11.810  17.499  -2.784  1.00 29.98 ? 21  LEU B CD2 1 
ATOM   3045 N N   . LEU B 1 21  ? 12.858  12.644  -0.511  1.00 29.76 ? 22  LEU B N   1 
ATOM   3046 C CA  . LEU B 1 21  ? 13.434  11.882  0.592   1.00 26.47 ? 22  LEU B CA  1 
ATOM   3047 C C   . LEU B 1 21  ? 14.937  11.703  0.407   1.00 30.89 ? 22  LEU B C   1 
ATOM   3048 O O   . LEU B 1 21  ? 15.697  11.762  1.380   1.00 30.78 ? 22  LEU B O   1 
ATOM   3049 C CB  . LEU B 1 21  ? 12.748  10.517  0.739   1.00 29.27 ? 22  LEU B CB  1 
ATOM   3050 C CG  . LEU B 1 21  ? 11.325  10.508  1.324   1.00 30.88 ? 22  LEU B CG  1 
ATOM   3051 C CD1 . LEU B 1 21  ? 10.352  10.097  0.249   1.00 35.34 ? 22  LEU B CD1 1 
ATOM   3052 C CD2 . LEU B 1 21  ? 11.214  9.545   2.528   1.00 30.91 ? 22  LEU B CD2 1 
ATOM   3053 N N   . GLU B 1 22  ? 15.385  11.488  -0.833  1.00 30.67 ? 23  GLU B N   1 
ATOM   3054 C CA  . GLU B 1 22  ? 16.816  11.329  -1.082  1.00 34.39 ? 23  GLU B CA  1 
ATOM   3055 C C   . GLU B 1 22  ? 17.551  12.660  -0.956  1.00 31.42 ? 23  GLU B C   1 
ATOM   3056 O O   . GLU B 1 22  ? 18.625  12.725  -0.345  1.00 35.44 ? 23  GLU B O   1 
ATOM   3057 C CB  . GLU B 1 22  ? 17.047  10.711  -2.462  1.00 35.13 ? 23  GLU B CB  1 
ATOM   3058 C CG  . GLU B 1 22  ? 18.456  10.916  -3.032  1.00 43.85 ? 23  GLU B CG  1 
ATOM   3059 C CD  . GLU B 1 22  ? 19.491  9.937   -2.482  1.00 51.49 ? 23  GLU B CD  1 
ATOM   3060 O OE1 . GLU B 1 22  ? 20.249  9.351   -3.293  1.00 55.05 ? 23  GLU B OE1 1 
ATOM   3061 O OE2 . GLU B 1 22  ? 19.555  9.752   -1.243  1.00 47.63 ? 23  GLU B OE2 1 
ATOM   3062 N N   . LYS B 1 23  ? 16.984  13.727  -1.515  1.00 30.53 ? 24  LYS B N   1 
ATOM   3063 C CA  . LYS B 1 23  ? 17.658  15.025  -1.523  1.00 31.69 ? 24  LYS B CA  1 
ATOM   3064 C C   . LYS B 1 23  ? 17.905  15.559  -0.109  1.00 31.03 ? 24  LYS B C   1 
ATOM   3065 O O   . LYS B 1 23  ? 18.949  16.173  0.155   1.00 32.52 ? 24  LYS B O   1 
ATOM   3066 C CB  . LYS B 1 23  ? 16.838  16.022  -2.345  1.00 31.80 ? 24  LYS B CB  1 
ATOM   3067 C CG  . LYS B 1 23  ? 17.399  17.440  -2.385  1.00 33.76 ? 24  LYS B CG  1 
ATOM   3068 C CD  . LYS B 1 23  ? 16.739  18.254  -3.487  1.00 33.51 ? 24  LYS B CD  1 
ATOM   3069 C CE  . LYS B 1 23  ? 17.223  19.699  -3.473  1.00 41.82 ? 24  LYS B CE  1 
ATOM   3070 N NZ  . LYS B 1 23  ? 16.638  20.500  -4.594  1.00 43.23 ? 24  LYS B NZ  1 
ATOM   3071 N N   . TYR B 1 24  ? 16.967  15.333  0.814   1.00 29.17 ? 25  TYR B N   1 
ATOM   3072 C CA  . TYR B 1 24  ? 17.047  15.880  2.166   1.00 29.23 ? 25  TYR B CA  1 
ATOM   3073 C C   . TYR B 1 24  ? 17.253  14.809  3.234   1.00 29.03 ? 25  TYR B C   1 
ATOM   3074 O O   . TYR B 1 24  ? 17.206  15.120  4.432   1.00 28.90 ? 25  TYR B O   1 
ATOM   3075 C CB  . TYR B 1 24  ? 15.787  16.707  2.467   1.00 29.85 ? 25  TYR B CB  1 
ATOM   3076 C CG  . TYR B 1 24  ? 15.680  17.908  1.554   1.00 29.29 ? 25  TYR B CG  1 
ATOM   3077 C CD1 . TYR B 1 24  ? 16.448  19.042  1.782   1.00 32.20 ? 25  TYR B CD1 1 
ATOM   3078 C CD2 . TYR B 1 24  ? 14.845  17.896  0.443   1.00 26.86 ? 25  TYR B CD2 1 
ATOM   3079 C CE1 . TYR B 1 24  ? 16.378  20.134  0.939   1.00 31.02 ? 25  TYR B CE1 1 
ATOM   3080 C CE2 . TYR B 1 24  ? 14.772  18.986  -0.410  1.00 31.81 ? 25  TYR B CE2 1 
ATOM   3081 C CZ  . TYR B 1 24  ? 15.540  20.098  -0.153  1.00 31.79 ? 25  TYR B CZ  1 
ATOM   3082 O OH  . TYR B 1 24  ? 15.477  21.180  -0.993  1.00 34.78 ? 25  TYR B OH  1 
ATOM   3083 N N   . ASP B 1 25  ? 17.509  13.570  2.831   1.00 27.38 ? 26  ASP B N   1 
ATOM   3084 C CA  . ASP B 1 25  ? 17.631  12.419  3.736   1.00 32.29 ? 26  ASP B CA  1 
ATOM   3085 C C   . ASP B 1 25  ? 16.515  12.423  4.786   1.00 28.60 ? 26  ASP B C   1 
ATOM   3086 O O   . ASP B 1 25  ? 16.748  12.419  5.994   1.00 28.50 ? 26  ASP B O   1 
ATOM   3087 C CB  . ASP B 1 25  ? 19.009  12.368  4.403   1.00 31.49 ? 26  ASP B CB  1 
ATOM   3088 C CG  . ASP B 1 25  ? 19.433  10.948  4.761   1.00 37.84 ? 26  ASP B CG  1 
ATOM   3089 O OD1 . ASP B 1 25  ? 18.546  10.098  5.015   1.00 40.34 ? 26  ASP B OD1 1 
ATOM   3090 O OD2 . ASP B 1 25  ? 20.656  10.670  4.775   1.00 42.02 ? 26  ASP B OD2 1 
ATOM   3091 N N   . VAL B 1 26  ? 15.285  12.430  4.296   1.00 26.39 ? 27  VAL B N   1 
ATOM   3092 C CA  . VAL B 1 26  ? 14.112  12.364  5.171   1.00 25.75 ? 27  VAL B CA  1 
ATOM   3093 C C   . VAL B 1 26  ? 13.936  10.924  5.648   1.00 26.31 ? 27  VAL B C   1 
ATOM   3094 O O   . VAL B 1 26  ? 13.869  10.011  4.812   1.00 25.16 ? 27  VAL B O   1 
ATOM   3095 C CB  . VAL B 1 26  ? 12.871  12.847  4.435   1.00 25.54 ? 27  VAL B CB  1 
ATOM   3096 C CG1 . VAL B 1 26  ? 11.628  12.760  5.348   1.00 23.31 ? 27  VAL B CG1 1 
ATOM   3097 C CG2 . VAL B 1 26  ? 13.085  14.282  3.934   1.00 23.71 ? 27  VAL B CG2 1 
ATOM   3098 N N   . PRO B 1 27  ? 13.871  10.678  6.959   1.00 26.64 ? 28  PRO B N   1 
ATOM   3099 C CA  . PRO B 1 27  ? 13.713  9.284   7.413   1.00 24.93 ? 28  PRO B CA  1 
ATOM   3100 C C   . PRO B 1 27  ? 12.417  8.637   6.952   1.00 24.82 ? 28  PRO B C   1 
ATOM   3101 O O   . PRO B 1 27  ? 12.449  7.482   6.502   1.00 26.70 ? 28  PRO B O   1 
ATOM   3102 C CB  . PRO B 1 27  ? 13.794  9.403   8.941   1.00 24.04 ? 28  PRO B CB  1 
ATOM   3103 C CG  . PRO B 1 27  ? 14.635  10.662  9.168   1.00 30.22 ? 28  PRO B CG  1 
ATOM   3104 C CD  . PRO B 1 27  ? 14.193  11.594  8.071   1.00 24.73 ? 28  PRO B CD  1 
ATOM   3105 N N   . GLY B 1 28  ? 11.289  9.337   7.041   1.00 23.27 ? 29  GLY B N   1 
ATOM   3106 C CA  . GLY B 1 28  ? 10.015  8.780   6.621   1.00 23.04 ? 29  GLY B CA  1 
ATOM   3107 C C   . GLY B 1 28  ? 9.038   9.842   6.160   1.00 23.38 ? 29  GLY B C   1 
ATOM   3108 O O   . GLY B 1 28  ? 9.148   11.032  6.503   1.00 22.65 ? 29  GLY B O   1 
ATOM   3109 N N   . MET B 1 29  ? 8.053   9.393   5.385   1.00 22.68 ? 30  MET B N   1 
ATOM   3110 C CA  . MET B 1 29  ? 7.085   10.313  4.796   1.00 22.27 ? 30  MET B CA  1 
ATOM   3111 C C   . MET B 1 29  ? 5.798   9.556   4.504   1.00 22.60 ? 30  MET B C   1 
ATOM   3112 O O   . MET B 1 29  ? 5.842   8.390   4.095   1.00 23.34 ? 30  MET B O   1 
ATOM   3113 C CB  . MET B 1 29  ? 7.629   10.936  3.502   1.00 22.67 ? 30  MET B CB  1 
ATOM   3114 C CG  . MET B 1 29  ? 6.649   11.859  2.775   1.00 24.91 ? 30  MET B CG  1 
ATOM   3115 S SD  . MET B 1 29  ? 7.213   12.427  1.134   1.00 29.30 ? 30  MET B SD  1 
ATOM   3116 C CE  . MET B 1 29  ? 8.758   13.243  1.454   1.00 30.68 ? 30  MET B CE  1 
ATOM   3117 N N   . ALA B 1 30  ? 4.660   10.219  4.715   1.00 22.60 ? 31  ALA B N   1 
ATOM   3118 C CA  . ALA B 1 30  ? 3.355   9.706   4.307   1.00 22.51 ? 31  ALA B CA  1 
ATOM   3119 C C   . ALA B 1 30  ? 2.681   10.759  3.442   1.00 22.32 ? 31  ALA B C   1 
ATOM   3120 O O   . ALA B 1 30  ? 2.471   11.887  3.904   1.00 22.94 ? 31  ALA B O   1 
ATOM   3121 C CB  . ALA B 1 30  ? 2.475   9.369   5.521   1.00 22.28 ? 31  ALA B CB  1 
ATOM   3122 N N   . VAL B 1 31  ? 2.335   10.403  2.197   1.00 23.03 ? 32  VAL B N   1 
ATOM   3123 C CA  . VAL B 1 31  ? 1.727   11.338  1.247   1.00 23.03 ? 32  VAL B CA  1 
ATOM   3124 C C   . VAL B 1 31  ? 0.427   10.747  0.740   1.00 23.70 ? 32  VAL B C   1 
ATOM   3125 O O   . VAL B 1 31  ? 0.396   9.593   0.290   1.00 24.51 ? 32  VAL B O   1 
ATOM   3126 C CB  . VAL B 1 31  ? 2.636   11.650  0.040   1.00 25.31 ? 32  VAL B CB  1 
ATOM   3127 C CG1 . VAL B 1 31  ? 2.037   12.786  -0.795  1.00 24.31 ? 32  VAL B CG1 1 
ATOM   3128 C CG2 . VAL B 1 31  ? 3.963   12.041  0.507   1.00 28.31 ? 32  VAL B CG2 1 
ATOM   3129 N N   . GLY B 1 32  ? -0.625  11.545  0.772   1.00 23.45 ? 33  GLY B N   1 
ATOM   3130 C CA  . GLY B 1 32  ? -1.932  11.091  0.355   1.00 24.13 ? 33  GLY B CA  1 
ATOM   3131 C C   . GLY B 1 32  ? -2.625  12.079  -0.560  1.00 24.28 ? 33  GLY B C   1 
ATOM   3132 O O   . GLY B 1 32  ? -2.455  13.290  -0.448  1.00 23.61 ? 33  GLY B O   1 
ATOM   3133 N N   . VAL B 1 33  ? -3.417  11.528  -1.471  1.00 25.27 ? 34  VAL B N   1 
ATOM   3134 C CA  . VAL B 1 33  ? -4.298  12.285  -2.351  1.00 25.68 ? 34  VAL B CA  1 
ATOM   3135 C C   . VAL B 1 33  ? -5.707  11.778  -2.105  1.00 26.26 ? 34  VAL B C   1 
ATOM   3136 O O   . VAL B 1 33  ? -5.921  10.569  -1.966  1.00 26.88 ? 34  VAL B O   1 
ATOM   3137 C CB  . VAL B 1 33  ? -3.917  12.121  -3.839  1.00 26.58 ? 34  VAL B CB  1 
ATOM   3138 C CG1 . VAL B 1 33  ? -4.953  12.764  -4.735  1.00 27.68 ? 34  VAL B CG1 1 
ATOM   3139 C CG2 . VAL B 1 33  ? -2.546  12.709  -4.117  1.00 26.09 ? 34  VAL B CG2 1 
ATOM   3140 N N   . ILE B 1 34  ? -6.670  12.692  -2.032  1.00 26.13 ? 35  ILE B N   1 
ATOM   3141 C CA  . ILE B 1 34  ? -8.075  12.313  -1.962  1.00 26.87 ? 35  ILE B CA  1 
ATOM   3142 C C   . ILE B 1 34  ? -8.803  13.018  -3.094  1.00 29.28 ? 35  ILE B C   1 
ATOM   3143 O O   . ILE B 1 34  ? -8.630  14.223  -3.300  1.00 28.69 ? 35  ILE B O   1 
ATOM   3144 C CB  . ILE B 1 34  ? -8.702  12.622  -0.584  1.00 29.53 ? 35  ILE B CB  1 
ATOM   3145 C CG1 . ILE B 1 34  ? -10.169 12.169  -0.541  1.00 32.84 ? 35  ILE B CG1 1 
ATOM   3146 C CG2 . ILE B 1 34  ? -8.561  14.107  -0.214  1.00 26.18 ? 35  ILE B CG2 1 
ATOM   3147 C CD1 . ILE B 1 34  ? -10.694 11.945  0.872   1.00 31.54 ? 35  ILE B CD1 1 
ATOM   3148 N N   . GLN B 1 35  ? -9.565  12.253  -3.863  1.00 29.06 ? 36  GLN B N   1 
ATOM   3149 C CA  . GLN B 1 35  ? -10.323 12.787  -4.983  1.00 33.80 ? 36  GLN B CA  1 
ATOM   3150 C C   . GLN B 1 35  ? -11.679 12.104  -4.978  1.00 36.01 ? 36  GLN B C   1 
ATOM   3151 O O   . GLN B 1 35  ? -11.749 10.875  -4.892  1.00 37.23 ? 36  GLN B O   1 
ATOM   3152 C CB  . GLN B 1 35  ? -9.594  12.550  -6.311  1.00 33.87 ? 36  GLN B CB  1 
ATOM   3153 C CG  . GLN B 1 35  ? -10.272 13.174  -7.530  1.00 37.72 ? 36  GLN B CG  1 
ATOM   3154 C CD  . GLN B 1 35  ? -9.617  12.765  -8.835  1.00 42.12 ? 36  GLN B CD  1 
ATOM   3155 O OE1 . GLN B 1 35  ? -9.307  11.591  -9.044  1.00 44.00 ? 36  GLN B OE1 1 
ATOM   3156 N NE2 . GLN B 1 35  ? -9.403  13.731  -9.722  1.00 39.75 ? 36  GLN B NE2 1 
ATOM   3157 N N   . ASN B 1 36  ? -12.752 12.890  -5.017  1.00 36.91 ? 37  ASN B N   1 
ATOM   3158 C CA  . ASN B 1 36  ? -14.109 12.345  -5.018  1.00 36.36 ? 37  ASN B CA  1 
ATOM   3159 C C   . ASN B 1 36  ? -14.267 11.252  -3.964  1.00 35.80 ? 37  ASN B C   1 
ATOM   3160 O O   . ASN B 1 36  ? -14.772 10.164  -4.236  1.00 38.48 ? 37  ASN B O   1 
ATOM   3161 C CB  . ASN B 1 36  ? -14.474 11.809  -6.401  1.00 41.55 ? 37  ASN B CB  1 
ATOM   3162 C CG  . ASN B 1 36  ? -14.538 12.898  -7.448  1.00 44.60 ? 37  ASN B CG  1 
ATOM   3163 O OD1 . ASN B 1 36  ? -15.239 13.896  -7.277  1.00 45.69 ? 37  ASN B OD1 1 
ATOM   3164 N ND2 . ASN B 1 36  ? -13.803 12.713  -8.545  1.00 42.59 ? 37  ASN B ND2 1 
ATOM   3165 N N   . ASN B 1 37  ? -13.763 11.525  -2.763  1.00 41.89 ? 38  ASN B N   1 
ATOM   3166 C CA  . ASN B 1 37  ? -13.843 10.641  -1.605  1.00 44.95 ? 38  ASN B CA  1 
ATOM   3167 C C   . ASN B 1 37  ? -13.012 9.357   -1.747  1.00 45.64 ? 38  ASN B C   1 
ATOM   3168 O O   . ASN B 1 37  ? -13.030 8.531   -0.826  1.00 46.07 ? 38  ASN B O   1 
ATOM   3169 C CB  . ASN B 1 37  ? -15.299 10.269  -1.282  1.00 50.10 ? 38  ASN B CB  1 
ATOM   3170 C CG  . ASN B 1 37  ? -15.519 9.952   0.184   1.00 54.14 ? 38  ASN B CG  1 
ATOM   3171 O OD1 . ASN B 1 37  ? -14.638 10.156  1.024   1.00 50.14 ? 38  ASN B OD1 1 
ATOM   3172 N ND2 . ASN B 1 37  ? -16.713 9.456   0.500   1.00 57.70 ? 38  ASN B ND2 1 
ATOM   3173 N N   . LYS B 1 38  ? -12.293 9.157   -2.859  1.00 38.74 ? 39  LYS B N   1 
ATOM   3174 C CA  . LYS B 1 38  ? -11.351 8.048   -3.002  1.00 37.44 ? 39  LYS B CA  1 
ATOM   3175 C C   . LYS B 1 38  ? -9.983  8.472   -2.463  1.00 33.96 ? 39  LYS B C   1 
ATOM   3176 O O   . LYS B 1 38  ? -9.484  9.546   -2.812  1.00 32.61 ? 39  LYS B O   1 
ATOM   3177 C CB  . LYS B 1 38  ? -11.217 7.627   -4.469  1.00 35.73 ? 39  LYS B CB  1 
ATOM   3178 C CG  . LYS B 1 38  ? -12.496 7.683   -5.314  1.00 43.28 ? 39  LYS B CG  1 
ATOM   3179 C CD  . LYS B 1 38  ? -12.154 7.972   -6.805  1.00 47.25 ? 39  LYS B CD  1 
ATOM   3180 C CE  . LYS B 1 38  ? -11.089 9.093   -6.937  1.00 34.56 ? 39  LYS B CE  1 
ATOM   3181 N NZ  . LYS B 1 38  ? -10.546 9.366   -8.286  1.00 44.15 ? 39  LYS B NZ  1 
ATOM   3182 N N   . LYS B 1 39  ? -9.372  7.625   -1.635  1.00 29.88 ? 40  LYS B N   1 
ATOM   3183 C CA  . LYS B 1 39  ? -8.103  7.927   -0.983  1.00 29.30 ? 40  LYS B CA  1 
ATOM   3184 C C   . LYS B 1 39  ? -6.956  7.137   -1.610  1.00 31.26 ? 40  LYS B C   1 
ATOM   3185 O O   . LYS B 1 39  ? -7.082  5.935   -1.885  1.00 29.98 ? 40  LYS B O   1 
ATOM   3186 C CB  . LYS B 1 39  ? -8.197  7.648   0.528   1.00 34.33 ? 40  LYS B CB  1 
ATOM   3187 C CG  . LYS B 1 39  ? -9.103  8.665   1.271   1.00 34.78 ? 40  LYS B CG  1 
ATOM   3188 C CD  . LYS B 1 39  ? -9.645  8.175   2.633   1.00 36.27 ? 40  LYS B CD  1 
ATOM   3189 C CE  . LYS B 1 39  ? -8.728  8.568   3.796   1.00 36.72 ? 40  LYS B CE  1 
ATOM   3190 N NZ  . LYS B 1 39  ? -9.226  8.197   5.191   1.00 35.07 ? 40  LYS B NZ  1 
ATOM   3191 N N   . TYR B 1 40  ? -5.833  7.819   -1.832  1.00 28.30 ? 41  TYR B N   1 
ATOM   3192 C CA  . TYR B 1 40  ? -4.634  7.221   -2.412  1.00 28.57 ? 41  TYR B CA  1 
ATOM   3193 C C   . TYR B 1 40  ? -3.474  7.524   -1.469  1.00 27.45 ? 41  TYR B C   1 
ATOM   3194 O O   . TYR B 1 40  ? -3.094  8.690   -1.309  1.00 26.59 ? 41  TYR B O   1 
ATOM   3195 C CB  . TYR B 1 40  ? -4.378  7.769   -3.821  1.00 29.06 ? 41  TYR B CB  1 
ATOM   3196 C CG  . TYR B 1 40  ? -5.573  7.618   -4.746  1.00 30.21 ? 41  TYR B CG  1 
ATOM   3197 C CD1 . TYR B 1 40  ? -6.604  8.551   -4.755  1.00 30.09 ? 41  TYR B CD1 1 
ATOM   3198 C CD2 . TYR B 1 40  ? -5.676  6.526   -5.590  1.00 39.97 ? 41  TYR B CD2 1 
ATOM   3199 C CE1 . TYR B 1 40  ? -7.708  8.399   -5.599  1.00 31.71 ? 41  TYR B CE1 1 
ATOM   3200 C CE2 . TYR B 1 40  ? -6.761  6.364   -6.429  1.00 40.70 ? 41  TYR B CE2 1 
ATOM   3201 C CZ  . TYR B 1 40  ? -7.775  7.296   -6.435  1.00 42.12 ? 41  TYR B CZ  1 
ATOM   3202 O OH  . TYR B 1 40  ? -8.845  7.094   -7.286  1.00 37.09 ? 41  TYR B OH  1 
ATOM   3203 N N   . GLU B 1 41  ? -2.927  6.487   -0.832  1.00 27.54 ? 42  GLU B N   1 
ATOM   3204 C CA  . GLU B 1 41  ? -1.993  6.635   0.283   1.00 26.61 ? 42  GLU B CA  1 
ATOM   3205 C C   . GLU B 1 41  ? -0.662  5.979   -0.047  1.00 26.89 ? 42  GLU B C   1 
ATOM   3206 O O   . GLU B 1 41  ? -0.618  4.774   -0.326  1.00 27.88 ? 42  GLU B O   1 
ATOM   3207 C CB  . GLU B 1 41  ? -2.576  6.010   1.549   1.00 29.66 ? 42  GLU B CB  1 
ATOM   3208 C CG  . GLU B 1 41  ? -3.759  6.787   2.099   1.00 27.68 ? 42  GLU B CG  1 
ATOM   3209 C CD  . GLU B 1 41  ? -4.500  6.035   3.169   1.00 36.17 ? 42  GLU B CD  1 
ATOM   3210 O OE1 . GLU B 1 41  ? -3.956  5.021   3.699   1.00 36.37 ? 42  GLU B OE1 1 
ATOM   3211 O OE2 . GLU B 1 41  ? -5.643  6.456   3.471   1.00 38.54 ? 42  GLU B OE2 1 
ATOM   3212 N N   . MET B 1 42  ? 0.418   6.754   0.027   1.00 26.21 ? 43  MET B N   1 
ATOM   3213 C CA  . MET B 1 42  ? 1.777   6.272   -0.193  1.00 26.43 ? 43  MET B CA  1 
ATOM   3214 C C   . MET B 1 42  ? 2.594   6.459   1.079   1.00 25.62 ? 43  MET B C   1 
ATOM   3215 O O   . MET B 1 42  ? 2.588   7.542   1.664   1.00 24.74 ? 43  MET B O   1 
ATOM   3216 C CB  . MET B 1 42  ? 2.454   7.010   -1.353  1.00 27.71 ? 43  MET B CB  1 
ATOM   3217 C CG  . MET B 1 42  ? 2.061   6.551   -2.760  1.00 33.98 ? 43  MET B CG  1 
ATOM   3218 S SD  . MET B 1 42  ? 0.304   6.650   -3.179  1.00 50.57 ? 43  MET B SD  1 
ATOM   3219 C CE  . MET B 1 42  ? -0.055  8.370   -2.823  1.00 35.24 ? 43  MET B CE  1 
ATOM   3220 N N   . TYR B 1 43  ? 3.296   5.403   1.499   1.00 26.01 ? 44  TYR B N   1 
ATOM   3221 C CA  . TYR B 1 43  ? 4.153   5.438   2.680   1.00 25.45 ? 44  TYR B CA  1 
ATOM   3222 C C   . TYR B 1 43  ? 5.592   5.128   2.288   1.00 25.83 ? 44  TYR B C   1 
ATOM   3223 O O   . TYR B 1 43  ? 5.848   4.183   1.534   1.00 26.73 ? 44  TYR B O   1 
ATOM   3224 C CB  . TYR B 1 43  ? 3.651   4.441   3.746   1.00 25.63 ? 44  TYR B CB  1 
ATOM   3225 C CG  . TYR B 1 43  ? 2.222   4.731   4.146   1.00 25.37 ? 44  TYR B CG  1 
ATOM   3226 C CD1 . TYR B 1 43  ? 1.934   5.797   4.988   1.00 24.45 ? 44  TYR B CD1 1 
ATOM   3227 C CD2 . TYR B 1 43  ? 1.160   3.961   3.662   1.00 28.47 ? 44  TYR B CD2 1 
ATOM   3228 C CE1 . TYR B 1 43  ? 0.631   6.095   5.353   1.00 25.14 ? 44  TYR B CE1 1 
ATOM   3229 C CE2 . TYR B 1 43  ? -0.169  4.246   4.032   1.00 27.04 ? 44  TYR B CE2 1 
ATOM   3230 C CZ  . TYR B 1 43  ? -0.414  5.324   4.875   1.00 26.74 ? 44  TYR B CZ  1 
ATOM   3231 O OH  . TYR B 1 43  ? -1.705  5.650   5.252   1.00 24.95 ? 44  TYR B OH  1 
ATOM   3232 N N   . TYR B 1 44  ? 6.535   5.916   2.815   1.00 25.22 ? 45  TYR B N   1 
ATOM   3233 C CA  . TYR B 1 44  ? 7.954   5.750   2.523   1.00 25.59 ? 45  TYR B CA  1 
ATOM   3234 C C   . TYR B 1 44  ? 8.767   5.723   3.811   1.00 25.24 ? 45  TYR B C   1 
ATOM   3235 O O   . TYR B 1 44  ? 8.482   6.471   4.752   1.00 24.46 ? 45  TYR B O   1 
ATOM   3236 C CB  . TYR B 1 44  ? 8.500   6.901   1.644   1.00 25.39 ? 45  TYR B CB  1 
ATOM   3237 C CG  . TYR B 1 44  ? 7.740   7.125   0.360   1.00 27.16 ? 45  TYR B CG  1 
ATOM   3238 C CD1 . TYR B 1 44  ? 7.998   6.352   -0.767  1.00 28.46 ? 45  TYR B CD1 1 
ATOM   3239 C CD2 . TYR B 1 44  ? 6.766   8.111   0.274   1.00 27.53 ? 45  TYR B CD2 1 
ATOM   3240 C CE1 . TYR B 1 44  ? 7.299   6.557   -1.952  1.00 31.60 ? 45  TYR B CE1 1 
ATOM   3241 C CE2 . TYR B 1 44  ? 6.059   8.321   -0.907  1.00 29.95 ? 45  TYR B CE2 1 
ATOM   3242 C CZ  . TYR B 1 44  ? 6.341   7.546   -2.016  1.00 33.31 ? 45  TYR B CZ  1 
ATOM   3243 O OH  . TYR B 1 44  ? 5.650   7.743   -3.188  1.00 32.35 ? 45  TYR B OH  1 
ATOM   3244 N N   . GLY B 1 45  ? 9.813   4.902   3.820   1.00 25.90 ? 46  GLY B N   1 
ATOM   3245 C CA  . GLY B 1 45  ? 10.841  5.004   4.845   1.00 26.90 ? 46  GLY B CA  1 
ATOM   3246 C C   . GLY B 1 45  ? 10.380  4.587   6.236   1.00 25.75 ? 46  GLY B C   1 
ATOM   3247 O O   . GLY B 1 45  ? 9.517   3.716   6.411   1.00 25.74 ? 46  GLY B O   1 
ATOM   3248 N N   . LEU B 1 46  ? 10.966  5.250   7.242   1.00 26.23 ? 47  LEU B N   1 
ATOM   3249 C CA  . LEU B 1 46  ? 10.994  4.764   8.613   1.00 25.31 ? 47  LEU B CA  1 
ATOM   3250 C C   . LEU B 1 46  ? 10.522  5.833   9.594   1.00 26.19 ? 47  LEU B C   1 
ATOM   3251 O O   . LEU B 1 46  ? 10.713  7.041   9.376   1.00 24.26 ? 47  LEU B O   1 
ATOM   3252 C CB  . LEU B 1 46  ? 12.415  4.312   8.983   1.00 26.21 ? 47  LEU B CB  1 
ATOM   3253 C CG  . LEU B 1 46  ? 13.060  3.285   8.042   1.00 27.49 ? 47  LEU B CG  1 
ATOM   3254 C CD1 . LEU B 1 46  ? 14.527  3.031   8.420   1.00 30.03 ? 47  LEU B CD1 1 
ATOM   3255 C CD2 . LEU B 1 46  ? 12.259  1.996   8.023   1.00 28.26 ? 47  LEU B CD2 1 
ATOM   3256 N N   . GLN B 1 47  ? 9.910   5.367   10.694  1.00 25.22 ? 48  GLN B N   1 
ATOM   3257 C CA  . GLN B 1 47  ? 9.355   6.273   11.703  1.00 27.95 ? 48  GLN B CA  1 
ATOM   3258 C C   . GLN B 1 47  ? 10.447  7.082   12.395  1.00 30.10 ? 48  GLN B C   1 
ATOM   3259 O O   . GLN B 1 47  ? 10.279  8.289   12.623  1.00 28.31 ? 48  GLN B O   1 
ATOM   3260 C CB  . GLN B 1 47  ? 8.538   5.486   12.737  1.00 28.03 ? 48  GLN B CB  1 
ATOM   3261 C CG  . GLN B 1 47  ? 7.238   4.901   12.171  1.00 24.86 ? 48  GLN B CG  1 
ATOM   3262 C CD  . GLN B 1 47  ? 6.308   4.301   13.222  1.00 29.75 ? 48  GLN B CD  1 
ATOM   3263 O OE1 . GLN B 1 47  ? 5.109   4.115   12.976  1.00 24.92 ? 48  GLN B OE1 1 
ATOM   3264 N NE2 . GLN B 1 47  ? 6.853   3.989   14.395  1.00 27.45 ? 48  GLN B NE2 1 
ATOM   3265 N N   . SER B 1 48  ? 11.556  6.438   12.752  1.00 26.55 ? 49  SER B N   1 
ATOM   3266 C CA  . SER B 1 48  ? 12.713  7.128   13.307  1.00 32.50 ? 49  SER B CA  1 
ATOM   3267 C C   . SER B 1 48  ? 13.981  6.355   12.966  1.00 29.94 ? 49  SER B C   1 
ATOM   3268 O O   . SER B 1 48  ? 13.951  5.153   12.686  1.00 33.69 ? 49  SER B O   1 
ATOM   3269 C CB  . SER B 1 48  ? 12.594  7.310   14.825  1.00 34.02 ? 49  SER B CB  1 
ATOM   3270 O OG  . SER B 1 48  ? 12.741  6.072   15.503  1.00 34.83 ? 49  SER B OG  1 
ATOM   3271 N N   . VAL B 1 49  ? 15.108  7.067   13.001  1.00 30.80 ? 50  VAL B N   1 
ATOM   3272 C CA  . VAL B 1 49  ? 16.407  6.428   12.794  1.00 31.58 ? 50  VAL B CA  1 
ATOM   3273 C C   . VAL B 1 49  ? 16.646  5.372   13.860  1.00 39.51 ? 50  VAL B C   1 
ATOM   3274 O O   . VAL B 1 49  ? 17.210  4.305   13.592  1.00 38.91 ? 50  VAL B O   1 
ATOM   3275 C CB  . VAL B 1 49  ? 17.527  7.484   12.782  1.00 36.01 ? 50  VAL B CB  1 
ATOM   3276 C CG1 . VAL B 1 49  ? 18.897  6.821   12.685  1.00 42.41 ? 50  VAL B CG1 1 
ATOM   3277 C CG2 . VAL B 1 49  ? 17.317  8.460   11.641  1.00 35.48 ? 50  VAL B CG2 1 
ATOM   3278 N N   . GLN B 1 50  ? 16.169  5.632   15.072  1.00 39.17 ? 51  GLN B N   1 
ATOM   3279 C CA  . GLN B 1 50  ? 16.433  4.757   16.206  1.00 35.87 ? 51  GLN B CA  1 
ATOM   3280 C C   . GLN B 1 50  ? 15.529  3.516   16.207  1.00 35.13 ? 51  GLN B C   1 
ATOM   3281 O O   . GLN B 1 50  ? 15.985  2.426   16.563  1.00 36.91 ? 51  GLN B O   1 
ATOM   3282 C CB  . GLN B 1 50  ? 16.289  5.582   17.489  1.00 39.96 ? 51  GLN B CB  1 
ATOM   3283 C CG  . GLN B 1 50  ? 15.040  6.503   17.474  1.00 46.13 ? 51  GLN B CG  1 
ATOM   3284 C CD  . GLN B 1 50  ? 15.281  8.032   17.230  1.00 47.83 ? 51  GLN B CD  1 
ATOM   3285 O OE1 . GLN B 1 50  ? 15.726  8.483   16.152  1.00 36.20 ? 51  GLN B OE1 1 
ATOM   3286 N NE2 . GLN B 1 50  ? 14.916  8.828   18.233  1.00 46.44 ? 51  GLN B NE2 1 
ATOM   3287 N N   . ASP B 1 51  ? 14.259  3.629   15.789  1.00 37.03 ? 52  ASP B N   1 
ATOM   3288 C CA  . ASP B 1 51  ? 13.403  2.443   15.806  1.00 36.55 ? 52  ASP B CA  1 
ATOM   3289 C C   . ASP B 1 51  ? 13.476  1.631   14.515  1.00 34.00 ? 52  ASP B C   1 
ATOM   3290 O O   . ASP B 1 51  ? 13.249  0.421   14.555  1.00 34.73 ? 52  ASP B O   1 
ATOM   3291 C CB  . ASP B 1 51  ? 11.937  2.808   16.157  1.00 33.99 ? 52  ASP B CB  1 
ATOM   3292 C CG  . ASP B 1 51  ? 11.139  3.514   15.022  1.00 36.87 ? 52  ASP B CG  1 
ATOM   3293 O OD1 . ASP B 1 51  ? 11.523  3.551   13.826  1.00 36.53 ? 52  ASP B OD1 1 
ATOM   3294 O OD2 . ASP B 1 51  ? 10.053  4.047   15.361  1.00 36.20 ? 52  ASP B OD2 1 
ATOM   3295 N N   . LYS B 1 52  ? 13.827  2.254   13.385  1.00 32.25 ? 53  LYS B N   1 
ATOM   3296 C CA  . LYS B 1 52  ? 13.936  1.564   12.094  1.00 30.12 ? 53  LYS B CA  1 
ATOM   3297 C C   . LYS B 1 52  ? 12.641  0.843   11.722  1.00 30.58 ? 53  LYS B C   1 
ATOM   3298 O O   . LYS B 1 52  ? 12.663  -0.225  11.088  1.00 31.15 ? 53  LYS B O   1 
ATOM   3299 C CB  . LYS B 1 52  ? 15.105  0.573   12.094  1.00 35.26 ? 53  LYS B CB  1 
ATOM   3300 C CG  . LYS B 1 52  ? 16.456  1.177   12.464  1.00 37.45 ? 53  LYS B CG  1 
ATOM   3301 C CD  . LYS B 1 52  ? 17.016  2.009   11.332  1.00 38.57 ? 53  LYS B CD  1 
ATOM   3302 C CE  . LYS B 1 52  ? 18.548  2.007   11.349  1.00 46.27 ? 53  LYS B CE  1 
ATOM   3303 N NZ  . LYS B 1 52  ? 19.102  2.327   12.700  1.00 45.56 ? 53  LYS B NZ  1 
ATOM   3304 N N   . LYS B 1 53  ? 11.511  1.389   12.147  1.00 31.35 ? 54  LYS B N   1 
ATOM   3305 C CA  . LYS B 1 53  ? 10.200  0.783   11.929  1.00 31.14 ? 54  LYS B CA  1 
ATOM   3306 C C   . LYS B 1 53  ? 9.531   1.436   10.727  1.00 28.35 ? 54  LYS B C   1 
ATOM   3307 O O   . LYS B 1 53  ? 9.507   2.667   10.619  1.00 25.64 ? 54  LYS B O   1 
ATOM   3308 C CB  . LYS B 1 53  ? 9.323   0.944   13.176  1.00 31.46 ? 54  LYS B CB  1 
ATOM   3309 C CG  . LYS B 1 53  ? 7.972   0.259   13.120  1.00 37.74 ? 54  LYS B CG  1 
ATOM   3310 C CD  . LYS B 1 53  ? 7.315   0.226   14.507  1.00 40.01 ? 54  LYS B CD  1 
ATOM   3311 C CE  . LYS B 1 53  ? 6.225   -0.839  14.580  1.00 42.23 ? 54  LYS B CE  1 
ATOM   3312 N NZ  . LYS B 1 53  ? 5.230   -0.679  13.485  1.00 42.23 ? 54  LYS B NZ  1 
ATOM   3313 N N   . ALA B 1 54  ? 8.976   0.612   9.839   1.00 27.42 ? 55  ALA B N   1 
ATOM   3314 C CA  . ALA B 1 54  ? 8.298   1.116   8.636   1.00 24.36 ? 55  ALA B CA  1 
ATOM   3315 C C   . ALA B 1 54  ? 7.206   2.137   8.952   1.00 26.27 ? 55  ALA B C   1 
ATOM   3316 O O   . ALA B 1 54  ? 6.358   1.906   9.816   1.00 26.00 ? 55  ALA B O   1 
ATOM   3317 C CB  . ALA B 1 54  ? 7.676   -0.055  7.877   1.00 26.85 ? 55  ALA B CB  1 
ATOM   3318 N N   . VAL B 1 55  ? 7.214   3.263   8.218   1.00 22.91 ? 56  VAL B N   1 
ATOM   3319 C CA  . VAL B 1 55  ? 6.054   4.148   8.215   1.00 23.53 ? 56  VAL B CA  1 
ATOM   3320 C C   . VAL B 1 55  ? 4.871   3.409   7.600   1.00 23.82 ? 56  VAL B C   1 
ATOM   3321 O O   . VAL B 1 55  ? 5.001   2.713   6.581   1.00 23.27 ? 56  VAL B O   1 
ATOM   3322 C CB  . VAL B 1 55  ? 6.354   5.446   7.442   1.00 24.73 ? 56  VAL B CB  1 
ATOM   3323 C CG1 . VAL B 1 55  ? 5.067   6.244   7.220   1.00 22.41 ? 56  VAL B CG1 1 
ATOM   3324 C CG2 . VAL B 1 55  ? 7.375   6.308   8.170   1.00 20.64 ? 56  VAL B CG2 1 
ATOM   3325 N N   . ASN B 1 56  ? 3.703   3.556   8.215   1.00 22.17 ? 57  ASN B N   1 
ATOM   3326 C CA  . ASN B 1 56  ? 2.494   2.889   7.729   1.00 22.55 ? 57  ASN B CA  1 
ATOM   3327 C C   . ASN B 1 56  ? 1.292   3.771   8.057   1.00 24.63 ? 57  ASN B C   1 
ATOM   3328 O O   . ASN B 1 56  ? 1.444   4.914   8.499   1.00 23.82 ? 57  ASN B O   1 
ATOM   3329 C CB  . ASN B 1 56  ? 2.386   1.491   8.352   1.00 24.99 ? 57  ASN B CB  1 
ATOM   3330 C CG  . ASN B 1 56  ? 2.244   1.559   9.854   1.00 28.14 ? 57  ASN B CG  1 
ATOM   3331 O OD1 . ASN B 1 56  ? 1.129   1.617   10.383  1.00 29.82 ? 57  ASN B OD1 1 
ATOM   3332 N ND2 . ASN B 1 56  ? 3.371   1.606   10.552  1.00 30.64 ? 57  ASN B ND2 1 
ATOM   3333 N N   . SER B 1 57  ? 0.083   3.238   7.846   1.00 24.90 ? 58  SER B N   1 
ATOM   3334 C CA  . SER B 1 57  ? -1.112  4.051   8.041   1.00 28.51 ? 58  SER B CA  1 
ATOM   3335 C C   . SER B 1 57  ? -1.381  4.385   9.508   1.00 28.22 ? 58  SER B C   1 
ATOM   3336 O O   . SER B 1 57  ? -2.156  5.306   9.781   1.00 30.64 ? 58  SER B O   1 
ATOM   3337 C CB  . SER B 1 57  ? -2.325  3.351   7.429   1.00 26.32 ? 58  SER B CB  1 
ATOM   3338 O OG  . SER B 1 57  ? -2.490  2.060   7.990   1.00 26.66 ? 58  SER B OG  1 
ATOM   3339 N N   . SER B 1 58  ? -0.766  3.674   10.454  1.00 29.46 ? 59  SER B N   1 
ATOM   3340 C CA  . SER B 1 58  ? -0.906  4.001   11.870  1.00 26.61 ? 59  SER B CA  1 
ATOM   3341 C C   . SER B 1 58  ? 0.111   5.036   12.360  1.00 27.96 ? 59  SER B C   1 
ATOM   3342 O O   . SER B 1 58  ? -0.010  5.498   13.499  1.00 26.78 ? 59  SER B O   1 
ATOM   3343 C CB  . SER B 1 58  ? -0.779  2.731   12.728  1.00 26.22 ? 59  SER B CB  1 
ATOM   3344 O OG  . SER B 1 58  ? -1.800  1.780   12.442  1.00 30.96 ? 59  SER B OG  1 
ATOM   3345 N N   . THR B 1 59  ? 1.105   5.407   11.546  1.00 25.20 ? 60  THR B N   1 
ATOM   3346 C CA  . THR B 1 59  ? 2.178   6.281   12.008  1.00 24.26 ? 60  THR B CA  1 
ATOM   3347 C C   . THR B 1 59  ? 1.653   7.678   12.328  1.00 24.66 ? 60  THR B C   1 
ATOM   3348 O O   . THR B 1 59  ? 0.936   8.291   11.529  1.00 25.01 ? 60  THR B O   1 
ATOM   3349 C CB  . THR B 1 59  ? 3.293   6.361   10.953  1.00 23.56 ? 60  THR B CB  1 
ATOM   3350 O OG1 . THR B 1 59  ? 3.796   5.034   10.699  1.00 24.29 ? 60  THR B OG1 1 
ATOM   3351 C CG2 . THR B 1 59  ? 4.448   7.279   11.416  1.00 22.47 ? 60  THR B CG2 1 
ATOM   3352 N N   . ILE B 1 60  ? 2.027   8.184   13.498  1.00 24.15 ? 61  ILE B N   1 
ATOM   3353 C CA  . ILE B 1 60  ? 1.592   9.496   13.987  1.00 23.41 ? 61  ILE B CA  1 
ATOM   3354 C C   . ILE B 1 60  ? 2.721   10.495  13.784  1.00 24.13 ? 61  ILE B C   1 
ATOM   3355 O O   . ILE B 1 60  ? 3.857   10.253  14.220  1.00 24.71 ? 61  ILE B O   1 
ATOM   3356 C CB  . ILE B 1 60  ? 1.184   9.415   15.471  1.00 24.46 ? 61  ILE B CB  1 
ATOM   3357 C CG1 . ILE B 1 60  ? -0.026  8.491   15.644  1.00 26.55 ? 61  ILE B CG1 1 
ATOM   3358 C CG2 . ILE B 1 60  ? 0.911   10.820  16.041  1.00 26.49 ? 61  ILE B CG2 1 
ATOM   3359 C CD1 . ILE B 1 60  ? -0.248  8.025   17.079  1.00 28.45 ? 61  ILE B CD1 1 
ATOM   3360 N N   . PHE B 1 61  ? 2.405   11.634  13.151  1.00 22.66 ? 62  PHE B N   1 
ATOM   3361 C CA  . PHE B 1 61  ? 3.367   12.684  12.856  1.00 21.08 ? 62  PHE B CA  1 
ATOM   3362 C C   . PHE B 1 61  ? 2.957   13.975  13.560  1.00 23.39 ? 62  PHE B C   1 
ATOM   3363 O O   . PHE B 1 61  ? 1.764   14.253  13.723  1.00 24.09 ? 62  PHE B O   1 
ATOM   3364 C CB  . PHE B 1 61  ? 3.447   12.991  11.350  1.00 21.13 ? 62  PHE B CB  1 
ATOM   3365 C CG  . PHE B 1 61  ? 4.006   11.873  10.492  1.00 22.08 ? 62  PHE B CG  1 
ATOM   3366 C CD1 . PHE B 1 61  ? 3.193   10.835  10.055  1.00 22.28 ? 62  PHE B CD1 1 
ATOM   3367 C CD2 . PHE B 1 61  ? 5.331   11.923  10.053  1.00 22.35 ? 62  PHE B CD2 1 
ATOM   3368 C CE1 . PHE B 1 61  ? 3.707   9.823   9.227   1.00 23.33 ? 62  PHE B CE1 1 
ATOM   3369 C CE2 . PHE B 1 61  ? 5.851   10.938  9.225   1.00 24.34 ? 62  PHE B CE2 1 
ATOM   3370 C CZ  . PHE B 1 61  ? 5.043   9.874   8.818   1.00 21.84 ? 62  PHE B CZ  1 
ATOM   3371 N N   . GLU B 1 62  ? 3.946   14.779  13.943  1.00 21.91 ? 63  GLU B N   1 
ATOM   3372 C CA  . GLU B 1 62  ? 3.671   16.144  14.398  1.00 20.06 ? 63  GLU B CA  1 
ATOM   3373 C C   . GLU B 1 62  ? 3.227   17.009  13.218  1.00 23.25 ? 63  GLU B C   1 
ATOM   3374 O O   . GLU B 1 62  ? 3.679   16.823  12.084  1.00 23.41 ? 63  GLU B O   1 
ATOM   3375 C CB  . GLU B 1 62  ? 4.913   16.737  15.077  1.00 24.90 ? 63  GLU B CB  1 
ATOM   3376 C CG  . GLU B 1 62  ? 5.305   16.007  16.361  1.00 28.64 ? 63  GLU B CG  1 
ATOM   3377 C CD  . GLU B 1 62  ? 6.554   16.554  17.061  1.00 36.89 ? 63  GLU B CD  1 
ATOM   3378 O OE1 . GLU B 1 62  ? 7.149   17.559  16.604  1.00 36.05 ? 63  GLU B OE1 1 
ATOM   3379 O OE2 . GLU B 1 62  ? 6.943   15.969  18.099  1.00 37.14 ? 63  GLU B OE2 1 
ATOM   3380 N N   . LEU B 1 63  ? 2.332   17.973  13.487  1.00 22.97 ? 64  LEU B N   1 
ATOM   3381 C CA  . LEU B 1 63  ? 1.775   18.839  12.444  1.00 20.46 ? 64  LEU B CA  1 
ATOM   3382 C C   . LEU B 1 63  ? 2.265   20.281  12.503  1.00 23.48 ? 64  LEU B C   1 
ATOM   3383 O O   . LEU B 1 63  ? 2.032   21.039  11.545  1.00 20.43 ? 64  LEU B O   1 
ATOM   3384 C CB  . LEU B 1 63  ? 0.238   18.843  12.520  1.00 21.72 ? 64  LEU B CB  1 
ATOM   3385 C CG  . LEU B 1 63  ? -0.555  17.536  12.426  1.00 22.20 ? 64  LEU B CG  1 
ATOM   3386 C CD1 . LEU B 1 63  ? -2.056  17.826  12.534  1.00 19.12 ? 64  LEU B CD1 1 
ATOM   3387 C CD2 . LEU B 1 63  ? -0.240  16.740  11.148  1.00 20.12 ? 64  LEU B CD2 1 
ATOM   3388 N N   . GLY B 1 64  ? 2.907   20.693  13.594  1.00 22.34 ? 65  GLY B N   1 
ATOM   3389 C CA  . GLY B 1 64  ? 3.313   22.094  13.696  1.00 23.63 ? 65  GLY B CA  1 
ATOM   3390 C C   . GLY B 1 64  ? 2.125   23.020  13.526  1.00 21.89 ? 65  GLY B C   1 
ATOM   3391 O O   . GLY B 1 64  ? 1.047   22.791  14.082  1.00 23.38 ? 65  GLY B O   1 
ATOM   3392 N N   . SER B 1 65  ? 2.316   24.056  12.701  1.00 22.04 ? 66  SER B N   1 
ATOM   3393 C CA  . SER B 1 65  ? 1.316   25.098  12.491  1.00 22.38 ? 66  SER B CA  1 
ATOM   3394 C C   . SER B 1 65  ? 0.045   24.595  11.821  1.00 22.71 ? 66  SER B C   1 
ATOM   3395 O O   . SER B 1 65  ? -0.963  25.298  11.855  1.00 19.56 ? 66  SER B O   1 
ATOM   3396 C CB  . SER B 1 65  ? 1.908   26.225  11.643  1.00 25.29 ? 66  SER B CB  1 
ATOM   3397 O OG  . SER B 1 65  ? 2.553   27.164  12.477  1.00 32.84 ? 66  SER B OG  1 
ATOM   3398 N N   . VAL B 1 66  ? 0.057   23.413  11.196  1.00 17.89 ? 67  VAL B N   1 
ATOM   3399 C CA  . VAL B 1 66  ? -1.203  22.884  10.684  1.00 18.43 ? 67  VAL B CA  1 
ATOM   3400 C C   . VAL B 1 66  ? -2.170  22.609  11.838  1.00 18.62 ? 67  VAL B C   1 
ATOM   3401 O O   . VAL B 1 66  ? -3.388  22.532  11.633  1.00 19.68 ? 67  VAL B O   1 
ATOM   3402 C CB  . VAL B 1 66  ? -0.937  21.631  9.803   1.00 21.55 ? 67  VAL B CB  1 
ATOM   3403 C CG1 . VAL B 1 66  ? -2.213  20.902  9.472   1.00 19.11 ? 67  VAL B CG1 1 
ATOM   3404 C CG2 . VAL B 1 66  ? -0.261  22.071  8.483   1.00 21.73 ? 67  VAL B CG2 1 
ATOM   3405 N N   . SER B 1 67  ? -1.657  22.513  13.069  1.00 18.96 ? 68  SER B N   1 
ATOM   3406 C CA  . SER B 1 67  ? -2.534  22.448  14.233  1.00 20.63 ? 68  SER B CA  1 
ATOM   3407 C C   . SER B 1 67  ? -3.517  23.609  14.263  1.00 22.26 ? 68  SER B C   1 
ATOM   3408 O O   . SER B 1 67  ? -4.639  23.465  14.768  1.00 21.62 ? 68  SER B O   1 
ATOM   3409 C CB  . SER B 1 67  ? -1.719  22.469  15.534  1.00 23.82 ? 68  SER B CB  1 
ATOM   3410 O OG  . SER B 1 67  ? -0.696  21.487  15.561  1.00 25.20 ? 68  SER B OG  1 
ATOM   3411 N N   . LYS B 1 68  ? -3.096  24.783  13.773  1.00 21.93 ? 69  LYS B N   1 
ATOM   3412 C CA  . LYS B 1 68  ? -3.947  25.967  13.816  1.00 19.58 ? 69  LYS B CA  1 
ATOM   3413 C C   . LYS B 1 68  ? -5.241  25.779  13.032  1.00 22.02 ? 69  LYS B C   1 
ATOM   3414 O O   . LYS B 1 68  ? -6.232  26.450  13.331  1.00 21.64 ? 69  LYS B O   1 
ATOM   3415 C CB  . LYS B 1 68  ? -3.185  27.175  13.276  1.00 21.20 ? 69  LYS B CB  1 
ATOM   3416 C CG  . LYS B 1 68  ? -1.930  27.568  14.081  1.00 25.03 ? 69  LYS B CG  1 
ATOM   3417 C CD  . LYS B 1 68  ? -1.212  28.764  13.411  1.00 24.95 ? 69  LYS B CD  1 
ATOM   3418 C CE  . LYS B 1 68  ? -0.081  29.320  14.275  1.00 27.21 ? 69  LYS B CE  1 
ATOM   3419 N NZ  . LYS B 1 68  ? 1.003   28.341  14.482  1.00 27.61 ? 69  LYS B NZ  1 
ATOM   3420 N N   . LEU B 1 69  ? -5.269  24.861  12.054  1.00 18.21 ? 70  LEU B N   1 
ATOM   3421 C CA  . LEU B 1 69  ? -6.530  24.576  11.372  1.00 21.37 ? 70  LEU B CA  1 
ATOM   3422 C C   . LEU B 1 69  ? -7.543  23.963  12.328  1.00 21.60 ? 70  LEU B C   1 
ATOM   3423 O O   . LEU B 1 69  ? -8.750  24.192  12.196  1.00 23.53 ? 70  LEU B O   1 
ATOM   3424 C CB  . LEU B 1 69  ? -6.305  23.640  10.176  1.00 19.26 ? 70  LEU B CB  1 
ATOM   3425 C CG  . LEU B 1 69  ? -5.226  24.072  9.177   1.00 21.78 ? 70  LEU B CG  1 
ATOM   3426 C CD1 . LEU B 1 69  ? -5.096  23.033  8.056   1.00 19.64 ? 70  LEU B CD1 1 
ATOM   3427 C CD2 . LEU B 1 69  ? -5.517  25.471  8.622   1.00 20.01 ? 70  LEU B CD2 1 
ATOM   3428 N N   . PHE B 1 70  ? -7.087  23.134  13.270  1.00 24.29 ? 71  PHE B N   1 
ATOM   3429 C CA  . PHE B 1 70  ? -8.041  22.563  14.212  1.00 23.01 ? 71  PHE B CA  1 
ATOM   3430 C C   . PHE B 1 70  ? -8.494  23.619  15.222  1.00 24.10 ? 71  PHE B C   1 
ATOM   3431 O O   . PHE B 1 70  ? -9.665  23.650  15.628  1.00 23.34 ? 71  PHE B O   1 
ATOM   3432 C CB  . PHE B 1 70  ? -7.435  21.331  14.899  1.00 25.67 ? 71  PHE B CB  1 
ATOM   3433 C CG  . PHE B 1 70  ? -7.212  20.182  13.955  1.00 25.22 ? 71  PHE B CG  1 
ATOM   3434 C CD1 . PHE B 1 70  ? -8.290  19.508  13.419  1.00 27.87 ? 71  PHE B CD1 1 
ATOM   3435 C CD2 . PHE B 1 70  ? -5.934  19.828  13.552  1.00 27.58 ? 71  PHE B CD2 1 
ATOM   3436 C CE1 . PHE B 1 70  ? -8.102  18.472  12.522  1.00 23.30 ? 71  PHE B CE1 1 
ATOM   3437 C CE2 . PHE B 1 70  ? -5.738  18.782  12.662  1.00 25.44 ? 71  PHE B CE2 1 
ATOM   3438 C CZ  . PHE B 1 70  ? -6.820  18.119  12.142  1.00 24.46 ? 71  PHE B CZ  1 
ATOM   3439 N N   . THR B 1 71  ? -7.584  24.506  15.616  1.00 23.51 ? 72  THR B N   1 
ATOM   3440 C CA  . THR B 1 71  ? -7.968  25.629  16.470  1.00 26.10 ? 72  THR B CA  1 
ATOM   3441 C C   . THR B 1 71  ? -9.007  26.513  15.785  1.00 24.38 ? 72  THR B C   1 
ATOM   3442 O O   . THR B 1 71  ? -10.002 26.921  16.402  1.00 27.05 ? 72  THR B O   1 
ATOM   3443 C CB  . THR B 1 71  ? -6.729  26.444  16.830  1.00 25.13 ? 72  THR B CB  1 
ATOM   3444 O OG1 . THR B 1 71  ? -5.758  25.592  17.459  1.00 26.16 ? 72  THR B OG1 1 
ATOM   3445 C CG2 . THR B 1 71  ? -7.095  27.610  17.764  1.00 29.60 ? 72  THR B CG2 1 
ATOM   3446 N N   . ALA B 1 72  ? -8.795  26.806  14.505  1.00 22.26 ? 73  ALA B N   1 
ATOM   3447 C CA  . ALA B 1 72  ? -9.755  27.593  13.740  1.00 26.17 ? 73  ALA B CA  1 
ATOM   3448 C C   . ALA B 1 72  ? -11.108 26.902  13.675  1.00 27.80 ? 73  ALA B C   1 
ATOM   3449 O O   . ALA B 1 72  ? -12.147 27.549  13.846  1.00 24.65 ? 73  ALA B O   1 
ATOM   3450 C CB  . ALA B 1 72  ? -9.215  27.845  12.333  1.00 21.23 ? 73  ALA B CB  1 
ATOM   3451 N N   . THR B 1 73  ? -11.115 25.582  13.430  1.00 24.20 ? 74  THR B N   1 
ATOM   3452 C CA  . THR B 1 73  ? -12.373 24.845  13.392  1.00 23.99 ? 74  THR B CA  1 
ATOM   3453 C C   . THR B 1 73  ? -13.082 24.914  14.733  1.00 27.75 ? 74  THR B C   1 
ATOM   3454 O O   . THR B 1 73  ? -14.310 25.047  14.794  1.00 28.05 ? 74  THR B O   1 
ATOM   3455 C CB  . THR B 1 73  ? -12.116 23.383  12.997  1.00 26.28 ? 74  THR B CB  1 
ATOM   3456 O OG1 . THR B 1 73  ? -11.415 23.348  11.747  1.00 25.12 ? 74  THR B OG1 1 
ATOM   3457 C CG2 . THR B 1 73  ? -13.429 22.627  12.869  1.00 28.00 ? 74  THR B CG2 1 
ATOM   3458 N N   . ALA B 1 74  ? -12.326 24.827  15.827  1.00 27.35 ? 75  ALA B N   1 
ATOM   3459 C CA  . ALA B 1 74  ? -12.965 24.881  17.133  1.00 30.16 ? 75  ALA B CA  1 
ATOM   3460 C C   . ALA B 1 74  ? -13.528 26.273  17.389  1.00 30.03 ? 75  ALA B C   1 
ATOM   3461 O O   . ALA B 1 74  ? -14.619 26.417  17.959  1.00 33.22 ? 75  ALA B O   1 
ATOM   3462 C CB  . ALA B 1 74  ? -11.969 24.465  18.219  1.00 28.46 ? 75  ALA B CB  1 
ATOM   3463 N N   . GLY B 1 75  ? -12.808 27.307  16.954  1.00 30.66 ? 76  GLY B N   1 
ATOM   3464 C CA  . GLY B 1 75  ? -13.357 28.650  17.017  1.00 30.82 ? 76  GLY B CA  1 
ATOM   3465 C C   . GLY B 1 75  ? -14.624 28.797  16.194  1.00 30.96 ? 76  GLY B C   1 
ATOM   3466 O O   . GLY B 1 75  ? -15.601 29.398  16.643  1.00 31.86 ? 76  GLY B O   1 
ATOM   3467 N N   . GLY B 1 76  ? -14.632 28.237  14.981  1.00 30.54 ? 77  GLY B N   1 
ATOM   3468 C CA  . GLY B 1 76  ? -15.853 28.256  14.187  1.00 33.20 ? 77  GLY B CA  1 
ATOM   3469 C C   . GLY B 1 76  ? -17.001 27.510  14.848  1.00 35.28 ? 77  GLY B C   1 
ATOM   3470 O O   . GLY B 1 76  ? -18.166 27.902  14.727  1.00 34.46 ? 77  GLY B O   1 
ATOM   3471 N N   . TYR B 1 77  ? -16.689 26.426  15.559  1.00 34.27 ? 78  TYR B N   1 
ATOM   3472 C CA  . TYR B 1 77  ? -17.720 25.646  16.243  1.00 34.25 ? 78  TYR B CA  1 
ATOM   3473 C C   . TYR B 1 77  ? -18.294 26.407  17.438  1.00 40.77 ? 78  TYR B C   1 
ATOM   3474 O O   . TYR B 1 77  ? -19.519 26.466  17.621  1.00 39.86 ? 78  TYR B O   1 
ATOM   3475 C CB  . TYR B 1 77  ? -17.124 24.308  16.676  1.00 35.01 ? 78  TYR B CB  1 
ATOM   3476 C CG  . TYR B 1 77  ? -18.067 23.331  17.332  1.00 39.95 ? 78  TYR B CG  1 
ATOM   3477 C CD1 . TYR B 1 77  ? -18.399 23.446  18.675  1.00 40.27 ? 78  TYR B CD1 1 
ATOM   3478 C CD2 . TYR B 1 77  ? -18.583 22.258  16.620  1.00 40.17 ? 78  TYR B CD2 1 
ATOM   3479 C CE1 . TYR B 1 77  ? -19.237 22.538  19.285  1.00 45.00 ? 78  TYR B CE1 1 
ATOM   3480 C CE2 . TYR B 1 77  ? -19.420 21.345  17.220  1.00 40.96 ? 78  TYR B CE2 1 
ATOM   3481 C CZ  . TYR B 1 77  ? -19.746 21.490  18.552  1.00 45.24 ? 78  TYR B CZ  1 
ATOM   3482 O OH  . TYR B 1 77  ? -20.582 20.580  19.151  1.00 51.72 ? 78  TYR B OH  1 
ATOM   3483 N N   . ALA B 1 78  ? -17.421 26.985  18.269  1.00 36.39 ? 79  ALA B N   1 
ATOM   3484 C CA  . ALA B 1 78  ? -17.880 27.797  19.393  1.00 37.06 ? 79  ALA B CA  1 
ATOM   3485 C C   . ALA B 1 78  ? -18.659 29.017  18.918  1.00 42.19 ? 79  ALA B C   1 
ATOM   3486 O O   . ALA B 1 78  ? -19.645 29.419  19.547  1.00 46.17 ? 79  ALA B O   1 
ATOM   3487 C CB  . ALA B 1 78  ? -16.690 28.238  20.246  1.00 39.84 ? 79  ALA B CB  1 
ATOM   3488 N N   . LYS B 1 79  ? -18.229 29.624  17.814  1.00 36.58 ? 80  LYS B N   1 
ATOM   3489 C CA  . LYS B 1 79  ? -18.925 30.796  17.296  1.00 40.79 ? 80  LYS B CA  1 
ATOM   3490 C C   . LYS B 1 79  ? -20.358 30.457  16.901  1.00 42.86 ? 80  LYS B C   1 
ATOM   3491 O O   . LYS B 1 79  ? -21.299 31.163  17.282  1.00 41.81 ? 80  LYS B O   1 
ATOM   3492 C CB  . LYS B 1 79  ? -18.158 31.376  16.105  1.00 38.22 ? 80  LYS B CB  1 
ATOM   3493 C CG  . LYS B 1 79  ? -18.763 32.637  15.520  1.00 42.13 ? 80  LYS B CG  1 
ATOM   3494 C CD  . LYS B 1 79  ? -19.552 32.347  14.259  1.00 42.09 ? 80  LYS B CD  1 
ATOM   3495 C CE  . LYS B 1 79  ? -19.983 33.629  13.569  1.00 43.93 ? 80  LYS B CE  1 
ATOM   3496 N NZ  . LYS B 1 79  ? -20.636 33.357  12.255  1.00 48.25 ? 80  LYS B NZ  1 
ATOM   3497 N N   . ASN B 1 80  ? -20.544 29.378  16.135  1.00 40.61 ? 81  ASN B N   1 
ATOM   3498 C CA  . ASN B 1 80  ? -21.859 29.084  15.578  1.00 41.06 ? 81  ASN B CA  1 
ATOM   3499 C C   . ASN B 1 80  ? -22.793 28.389  16.561  1.00 43.00 ? 81  ASN B C   1 
ATOM   3500 O O   . ASN B 1 80  ? -23.969 28.207  16.234  1.00 45.95 ? 81  ASN B O   1 
ATOM   3501 C CB  . ASN B 1 80  ? -21.729 28.239  14.308  1.00 43.50 ? 81  ASN B CB  1 
ATOM   3502 C CG  . ASN B 1 80  ? -21.313 29.060  13.098  1.00 43.99 ? 81  ASN B CG  1 
ATOM   3503 O OD1 . ASN B 1 80  ? -22.131 29.756  12.492  1.00 46.25 ? 81  ASN B OD1 1 
ATOM   3504 N ND2 . ASN B 1 80  ? -20.028 28.980  12.735  1.00 42.31 ? 81  ASN B ND2 1 
ATOM   3505 N N   . LYS B 1 81  ? -22.320 28.000  17.746  1.00 43.09 ? 82  LYS B N   1 
ATOM   3506 C CA  . LYS B 1 81  ? -23.213 27.613  18.830  1.00 47.30 ? 82  LYS B CA  1 
ATOM   3507 C C   . LYS B 1 81  ? -23.369 28.721  19.876  1.00 48.39 ? 82  LYS B C   1 
ATOM   3508 O O   . LYS B 1 81  ? -23.817 28.454  20.996  1.00 51.43 ? 82  LYS B O   1 
ATOM   3509 C CB  . LYS B 1 81  ? -22.742 26.315  19.487  1.00 47.86 ? 82  LYS B CB  1 
ATOM   3510 C CG  . LYS B 1 81  ? -22.893 25.096  18.600  1.00 48.05 ? 82  LYS B CG  1 
ATOM   3511 C CD  . LYS B 1 81  ? -23.286 23.855  19.399  1.00 56.27 ? 82  LYS B CD  1 
ATOM   3512 C CE  . LYS B 1 81  ? -22.344 23.621  20.568  1.00 55.56 ? 82  LYS B CE  1 
ATOM   3513 N NZ  . LYS B 1 81  ? -22.690 22.382  21.294  1.00 59.00 ? 82  LYS B NZ  1 
ATOM   3514 N N   . GLY B 1 82  ? -23.005 29.956  19.532  1.00 48.79 ? 83  GLY B N   1 
ATOM   3515 C CA  . GLY B 1 82  ? -23.230 31.074  20.425  1.00 45.11 ? 83  GLY B CA  1 
ATOM   3516 C C   . GLY B 1 82  ? -22.392 31.095  21.685  1.00 48.77 ? 83  GLY B C   1 
ATOM   3517 O O   . GLY B 1 82  ? -22.743 31.801  22.634  1.00 48.49 ? 83  GLY B O   1 
ATOM   3518 N N   . LYS B 1 83  ? -21.286 30.348  21.728  1.00 45.54 ? 84  LYS B N   1 
ATOM   3519 C CA  . LYS B 1 83  ? -20.411 30.423  22.892  1.00 45.09 ? 84  LYS B CA  1 
ATOM   3520 C C   . LYS B 1 83  ? -19.498 31.642  22.831  1.00 47.91 ? 84  LYS B C   1 
ATOM   3521 O O   . LYS B 1 83  ? -19.077 32.150  23.876  1.00 46.82 ? 84  LYS B O   1 
ATOM   3522 C CB  . LYS B 1 83  ? -19.580 29.144  23.021  1.00 47.96 ? 84  LYS B CB  1 
ATOM   3523 C CG  . LYS B 1 83  ? -20.393 27.869  23.250  1.00 48.82 ? 84  LYS B CG  1 
ATOM   3524 C CD  . LYS B 1 83  ? -21.280 28.008  24.470  1.00 55.52 ? 84  LYS B CD  1 
ATOM   3525 C CE  . LYS B 1 83  ? -21.714 26.658  25.011  1.00 55.86 ? 84  LYS B CE  1 
ATOM   3526 N NZ  . LYS B 1 83  ? -22.556 26.822  26.230  1.00 54.76 ? 84  LYS B NZ  1 
ATOM   3527 N N   . ILE B 1 84  ? -19.185 32.121  21.624  1.00 47.57 ? 85  ILE B N   1 
ATOM   3528 C CA  . ILE B 1 84  ? -18.438 33.355  21.428  1.00 41.02 ? 85  ILE B CA  1 
ATOM   3529 C C   . ILE B 1 84  ? -19.040 34.106  20.254  1.00 40.76 ? 85  ILE B C   1 
ATOM   3530 O O   . ILE B 1 84  ? -19.795 33.556  19.450  1.00 41.60 ? 85  ILE B O   1 
ATOM   3531 C CB  . ILE B 1 84  ? -16.934 33.127  21.151  1.00 41.05 ? 85  ILE B CB  1 
ATOM   3532 C CG1 . ILE B 1 84  ? -16.749 32.193  19.946  1.00 40.16 ? 85  ILE B CG1 1 
ATOM   3533 C CG2 . ILE B 1 84  ? -16.215 32.627  22.385  1.00 41.59 ? 85  ILE B CG2 1 
ATOM   3534 C CD1 . ILE B 1 84  ? -15.285 31.932  19.568  1.00 39.19 ? 85  ILE B CD1 1 
ATOM   3535 N N   . SER B 1 85  ? -18.700 35.388  20.183  1.00 39.79 ? 86  SER B N   1 
ATOM   3536 C CA  . SER B 1 85  ? -18.833 36.208  18.988  1.00 39.59 ? 86  SER B CA  1 
ATOM   3537 C C   . SER B 1 85  ? -17.439 36.675  18.593  1.00 37.72 ? 86  SER B C   1 
ATOM   3538 O O   . SER B 1 85  ? -16.616 36.979  19.464  1.00 37.23 ? 86  SER B O   1 
ATOM   3539 C CB  . SER B 1 85  ? -19.751 37.415  19.238  1.00 40.38 ? 86  SER B CB  1 
ATOM   3540 O OG  . SER B 1 85  ? -19.588 38.407  18.237  1.00 46.47 ? 86  SER B OG  1 
ATOM   3541 N N   . PHE B 1 86  ? -17.151 36.718  17.290  1.00 34.90 ? 87  PHE B N   1 
ATOM   3542 C CA  . PHE B 1 86  ? -15.811 37.155  16.897  1.00 32.44 ? 87  PHE B CA  1 
ATOM   3543 C C   . PHE B 1 86  ? -15.566 38.633  17.206  1.00 34.75 ? 87  PHE B C   1 
ATOM   3544 O O   . PHE B 1 86  ? -14.423 39.094  17.097  1.00 33.43 ? 87  PHE B O   1 
ATOM   3545 C CB  . PHE B 1 86  ? -15.564 36.868  15.409  1.00 28.57 ? 87  PHE B CB  1 
ATOM   3546 C CG  . PHE B 1 86  ? -15.428 35.401  15.084  1.00 31.47 ? 87  PHE B CG  1 
ATOM   3547 C CD1 . PHE B 1 86  ? -15.067 34.485  16.064  1.00 33.10 ? 87  PHE B CD1 1 
ATOM   3548 C CD2 . PHE B 1 86  ? -15.667 34.935  13.798  1.00 36.43 ? 87  PHE B CD2 1 
ATOM   3549 C CE1 . PHE B 1 86  ? -14.938 33.119  15.758  1.00 35.40 ? 87  PHE B CE1 1 
ATOM   3550 C CE2 . PHE B 1 86  ? -15.541 33.581  13.481  1.00 34.14 ? 87  PHE B CE2 1 
ATOM   3551 C CZ  . PHE B 1 86  ? -15.177 32.673  14.462  1.00 34.99 ? 87  PHE B CZ  1 
ATOM   3552 N N   . ASP B 1 87  ? -16.596 39.377  17.599  1.00 35.77 ? 88  ASP B N   1 
ATOM   3553 C CA  . ASP B 1 87  ? -16.435 40.760  18.038  1.00 38.19 ? 88  ASP B CA  1 
ATOM   3554 C C   . ASP B 1 87  ? -16.136 40.887  19.526  1.00 37.36 ? 88  ASP B C   1 
ATOM   3555 O O   . ASP B 1 87  ? -15.894 42.003  19.996  1.00 43.65 ? 88  ASP B O   1 
ATOM   3556 C CB  . ASP B 1 87  ? -17.692 41.577  17.724  1.00 42.49 ? 88  ASP B CB  1 
ATOM   3557 C CG  . ASP B 1 87  ? -17.879 41.817  16.242  1.00 49.01 ? 88  ASP B CG  1 
ATOM   3558 O OD1 . ASP B 1 87  ? -16.870 41.865  15.507  1.00 44.95 ? 88  ASP B OD1 1 
ATOM   3559 O OD2 . ASP B 1 87  ? -19.042 41.964  15.813  1.00 55.76 ? 88  ASP B OD2 1 
ATOM   3560 N N   . ASP B 1 88  ? -16.174 39.793  20.277  1.00 37.46 ? 89  ASP B N   1 
ATOM   3561 C CA  . ASP B 1 88  ? -15.837 39.843  21.692  1.00 42.70 ? 89  ASP B CA  1 
ATOM   3562 C C   . ASP B 1 88  ? -14.341 40.083  21.866  1.00 39.71 ? 89  ASP B C   1 
ATOM   3563 O O   . ASP B 1 88  ? -13.538 39.849  20.960  1.00 37.84 ? 89  ASP B O   1 
ATOM   3564 C CB  . ASP B 1 88  ? -16.224 38.534  22.396  1.00 36.65 ? 89  ASP B CB  1 
ATOM   3565 C CG  . ASP B 1 88  ? -17.727 38.324  22.474  1.00 45.56 ? 89  ASP B CG  1 
ATOM   3566 O OD1 . ASP B 1 88  ? -18.476 39.274  22.161  1.00 43.56 ? 89  ASP B OD1 1 
ATOM   3567 O OD2 . ASP B 1 88  ? -18.152 37.199  22.839  1.00 45.54 ? 89  ASP B OD2 1 
ATOM   3568 N N   . THR B 1 89  ? -13.969 40.537  23.052  1.00 40.49 ? 90  THR B N   1 
ATOM   3569 C CA  . THR B 1 89  ? -12.569 40.710  23.404  1.00 38.69 ? 90  THR B CA  1 
ATOM   3570 C C   . THR B 1 89  ? -12.165 39.681  24.458  1.00 41.69 ? 90  THR B C   1 
ATOM   3571 O O   . THR B 1 89  ? -13.026 39.094  25.123  1.00 41.82 ? 90  THR B O   1 
ATOM   3572 C CB  . THR B 1 89  ? -12.321 42.136  23.914  1.00 38.36 ? 90  THR B CB  1 
ATOM   3573 O OG1 . THR B 1 89  ? -13.090 42.374  25.100  1.00 40.27 ? 90  THR B OG1 1 
ATOM   3574 C CG2 . THR B 1 89  ? -12.700 43.155  22.840  1.00 39.38 ? 90  THR B CG2 1 
ATOM   3575 N N   . PRO B 1 90  ? -10.861 39.414  24.620  1.00 40.48 ? 91  PRO B N   1 
ATOM   3576 C CA  . PRO B 1 90  ? -10.450 38.298  25.493  1.00 37.99 ? 91  PRO B CA  1 
ATOM   3577 C C   . PRO B 1 90  ? -10.875 38.448  26.946  1.00 46.79 ? 91  PRO B C   1 
ATOM   3578 O O   . PRO B 1 90  ? -11.138 37.435  27.613  1.00 45.57 ? 91  PRO B O   1 
ATOM   3579 C CB  . PRO B 1 90  ? -8.919  38.295  25.356  1.00 38.84 ? 91  PRO B CB  1 
ATOM   3580 C CG  . PRO B 1 90  ? -8.568  39.660  24.825  1.00 39.53 ? 91  PRO B CG  1 
ATOM   3581 C CD  . PRO B 1 90  ? -9.706  40.020  23.938  1.00 37.16 ? 91  PRO B CD  1 
ATOM   3582 N N   . GLY B 1 91  ? -10.953 39.679  27.460  1.00 42.76 ? 92  GLY B N   1 
ATOM   3583 C CA  . GLY B 1 91  ? -11.289 39.884  28.860  1.00 49.57 ? 92  GLY B CA  1 
ATOM   3584 C C   . GLY B 1 91  ? -12.711 39.505  29.218  1.00 48.88 ? 92  GLY B C   1 
ATOM   3585 O O   . GLY B 1 91  ? -13.027 39.374  30.406  1.00 51.60 ? 92  GLY B O   1 
ATOM   3586 N N   . LYS B 1 92  ? -13.579 39.334  28.219  1.00 47.52 ? 93  LYS B N   1 
ATOM   3587 C CA  . LYS B 1 92  ? -14.921 38.830  28.477  1.00 48.93 ? 93  LYS B CA  1 
ATOM   3588 C C   . LYS B 1 92  ? -14.903 37.387  28.966  1.00 46.32 ? 93  LYS B C   1 
ATOM   3589 O O   . LYS B 1 92  ? -15.825 36.971  29.676  1.00 48.48 ? 93  LYS B O   1 
ATOM   3590 C CB  . LYS B 1 92  ? -15.775 38.962  27.213  1.00 48.11 ? 93  LYS B CB  1 
ATOM   3591 C CG  . LYS B 1 92  ? -17.109 38.230  27.258  1.00 46.40 ? 93  LYS B CG  1 
ATOM   3592 C CD  . LYS B 1 92  ? -18.023 38.749  26.170  1.00 51.63 ? 93  LYS B CD  1 
ATOM   3593 C CE  . LYS B 1 92  ? -19.350 38.019  26.159  1.00 52.98 ? 93  LYS B CE  1 
ATOM   3594 N NZ  . LYS B 1 92  ? -20.198 38.540  25.053  1.00 60.87 ? 93  LYS B NZ  1 
ATOM   3595 N N   . TYR B 1 93  ? -13.864 36.625  28.635  1.00 45.15 ? 94  TYR B N   1 
ATOM   3596 C CA  . TYR B 1 93  ? -13.757 35.228  29.033  1.00 48.01 ? 94  TYR B CA  1 
ATOM   3597 C C   . TYR B 1 93  ? -12.621 34.968  30.007  1.00 48.04 ? 94  TYR B C   1 
ATOM   3598 O O   . TYR B 1 93  ? -12.788 34.191  30.942  1.00 47.68 ? 94  TYR B O   1 
ATOM   3599 C CB  . TYR B 1 93  ? -13.598 34.348  27.784  1.00 45.60 ? 94  TYR B CB  1 
ATOM   3600 C CG  . TYR B 1 93  ? -14.740 34.571  26.823  1.00 45.03 ? 94  TYR B CG  1 
ATOM   3601 C CD1 . TYR B 1 93  ? -15.931 33.892  26.983  1.00 46.03 ? 94  TYR B CD1 1 
ATOM   3602 C CD2 . TYR B 1 93  ? -14.648 35.512  25.794  1.00 43.45 ? 94  TYR B CD2 1 
ATOM   3603 C CE1 . TYR B 1 93  ? -16.995 34.102  26.139  1.00 46.92 ? 94  TYR B CE1 1 
ATOM   3604 C CE2 . TYR B 1 93  ? -15.715 35.733  24.934  1.00 43.05 ? 94  TYR B CE2 1 
ATOM   3605 C CZ  . TYR B 1 93  ? -16.889 35.014  25.119  1.00 43.78 ? 94  TYR B CZ  1 
ATOM   3606 O OH  . TYR B 1 93  ? -17.974 35.201  24.297  1.00 45.02 ? 94  TYR B OH  1 
ATOM   3607 N N   . TRP B 1 94  ? -11.474 35.609  29.823  1.00 47.50 ? 95  TRP B N   1 
ATOM   3608 C CA  . TRP B 1 94  ? -10.358 35.509  30.758  1.00 46.50 ? 95  TRP B CA  1 
ATOM   3609 C C   . TRP B 1 94  ? -10.371 36.793  31.581  1.00 52.31 ? 95  TRP B C   1 
ATOM   3610 O O   . TRP B 1 94  ? -9.812  37.815  31.168  1.00 47.83 ? 95  TRP B O   1 
ATOM   3611 C CB  . TRP B 1 94  ? -9.046  35.300  30.009  1.00 45.21 ? 95  TRP B CB  1 
ATOM   3612 C CG  . TRP B 1 94  ? -7.894  34.924  30.882  1.00 45.88 ? 95  TRP B CG  1 
ATOM   3613 C CD1 . TRP B 1 94  ? -7.899  34.812  32.238  1.00 48.57 ? 95  TRP B CD1 1 
ATOM   3614 C CD2 . TRP B 1 94  ? -6.561  34.610  30.456  1.00 42.91 ? 95  TRP B CD2 1 
ATOM   3615 N NE1 . TRP B 1 94  ? -6.653  34.441  32.687  1.00 50.84 ? 95  TRP B NE1 1 
ATOM   3616 C CE2 . TRP B 1 94  ? -5.815  34.310  31.612  1.00 46.60 ? 95  TRP B CE2 1 
ATOM   3617 C CE3 . TRP B 1 94  ? -5.932  34.542  29.210  1.00 43.92 ? 95  TRP B CE3 1 
ATOM   3618 C CZ2 . TRP B 1 94  ? -4.470  33.953  31.560  1.00 49.53 ? 95  TRP B CZ2 1 
ATOM   3619 C CZ3 . TRP B 1 94  ? -4.594  34.191  29.159  1.00 45.48 ? 95  TRP B CZ3 1 
ATOM   3620 C CH2 . TRP B 1 94  ? -3.877  33.903  30.327  1.00 49.17 ? 95  TRP B CH2 1 
ATOM   3621 N N   . LYS B 1 95  ? -11.013 36.726  32.757  1.00 47.73 ? 96  LYS B N   1 
ATOM   3622 C CA  . LYS B 1 95  ? -11.416 37.928  33.489  1.00 51.94 ? 96  LYS B CA  1 
ATOM   3623 C C   . LYS B 1 95  ? -10.226 38.752  33.962  1.00 47.92 ? 96  LYS B C   1 
ATOM   3624 O O   . LYS B 1 95  ? -10.323 39.985  34.064  1.00 48.28 ? 96  LYS B O   1 
ATOM   3625 C CB  . LYS B 1 95  ? -12.294 37.537  34.683  1.00 59.02 ? 96  LYS B CB  1 
ATOM   3626 C CG  . LYS B 1 95  ? -13.579 36.822  34.291  1.00 59.25 ? 96  LYS B CG  1 
ATOM   3627 C CD  . LYS B 1 95  ? -14.384 37.680  33.320  1.00 63.70 ? 96  LYS B CD  1 
ATOM   3628 C CE  . LYS B 1 95  ? -15.720 37.033  32.969  1.00 68.28 ? 96  LYS B CE  1 
ATOM   3629 N NZ  . LYS B 1 95  ? -16.547 37.932  32.105  1.00 65.32 ? 96  LYS B NZ  1 
ATOM   3630 N N   . GLU B 1 96  ? -9.096  38.104  34.243  1.00 47.83 ? 97  GLU B N   1 
ATOM   3631 C CA  . GLU B 1 96  ? -7.896  38.825  34.643  1.00 48.12 ? 97  GLU B CA  1 
ATOM   3632 C C   . GLU B 1 96  ? -7.409  39.816  33.577  1.00 50.66 ? 97  GLU B C   1 
ATOM   3633 O O   . GLU B 1 96  ? -6.555  40.659  33.882  1.00 46.23 ? 97  GLU B O   1 
ATOM   3634 C CB  . GLU B 1 96  ? -6.805  37.809  35.003  1.00 48.33 ? 97  GLU B CB  1 
ATOM   3635 C CG  . GLU B 1 96  ? -6.979  37.160  36.390  1.00 51.25 ? 97  GLU B CG  1 
ATOM   3636 C CD  . GLU B 1 96  ? -8.131  36.147  36.480  1.00 59.78 ? 97  GLU B CD  1 
ATOM   3637 O OE1 . GLU B 1 96  ? -8.461  35.485  35.457  1.00 55.65 ? 97  GLU B OE1 1 
ATOM   3638 O OE2 . GLU B 1 96  ? -8.695  35.998  37.597  1.00 56.13 ? 97  GLU B OE2 1 
ATOM   3639 N N   . LEU B 1 97  ? -7.948  39.755  32.352  1.00 46.01 ? 98  LEU B N   1 
ATOM   3640 C CA  . LEU B 1 97  ? -7.573  40.656  31.264  1.00 44.49 ? 98  LEU B CA  1 
ATOM   3641 C C   . LEU B 1 97  ? -8.525  41.832  31.078  1.00 48.90 ? 98  LEU B C   1 
ATOM   3642 O O   . LEU B 1 97  ? -8.255  42.692  30.229  1.00 45.66 ? 98  LEU B O   1 
ATOM   3643 C CB  . LEU B 1 97  ? -7.498  39.891  29.946  1.00 43.17 ? 98  LEU B CB  1 
ATOM   3644 C CG  . LEU B 1 97  ? -6.525  38.724  29.948  1.00 46.34 ? 98  LEU B CG  1 
ATOM   3645 C CD1 . LEU B 1 97  ? -6.631  37.967  28.636  1.00 48.18 ? 98  LEU B CD1 1 
ATOM   3646 C CD2 . LEU B 1 97  ? -5.116  39.227  30.181  1.00 41.85 ? 98  LEU B CD2 1 
ATOM   3647 N N   . LYS B 1 98  ? -9.624  41.877  31.825  1.00 50.30 ? 99  LYS B N   1 
ATOM   3648 C CA  . LYS B 1 98  ? -10.603 42.948  31.684  1.00 53.54 ? 99  LYS B CA  1 
ATOM   3649 C C   . LYS B 1 98  ? -9.963  44.315  31.896  1.00 52.23 ? 99  LYS B C   1 
ATOM   3650 O O   . LYS B 1 98  ? -9.134  44.499  32.791  1.00 50.32 ? 99  LYS B O   1 
ATOM   3651 C CB  . LYS B 1 98  ? -11.735 42.748  32.692  1.00 56.94 ? 99  LYS B CB  1 
ATOM   3652 C CG  . LYS B 1 98  ? -12.864 41.856  32.218  1.00 61.25 ? 99  LYS B CG  1 
ATOM   3653 C CD  . LYS B 1 98  ? -13.809 42.612  31.298  1.00 64.09 ? 99  LYS B CD  1 
ATOM   3654 C CE  . LYS B 1 98  ? -14.210 43.944  31.919  1.00 67.35 ? 99  LYS B CE  1 
ATOM   3655 N NZ  . LYS B 1 98  ? -15.471 44.482  31.346  1.00 74.49 ? 99  LYS B NZ  1 
ATOM   3656 N N   . ASN B 1 99  ? -10.346 45.274  31.053  1.00 54.74 ? 100 ASN B N   1 
ATOM   3657 C CA  . ASN B 1 99  ? -9.903  46.665  31.149  1.00 55.84 ? 100 ASN B CA  1 
ATOM   3658 C C   . ASN B 1 99  ? -8.393  46.827  30.984  1.00 56.60 ? 100 ASN B C   1 
ATOM   3659 O O   . ASN B 1 99  ? -7.826  47.842  31.406  1.00 52.20 ? 100 ASN B O   1 
ATOM   3660 C CB  . ASN B 1 99  ? -10.355 47.297  32.469  1.00 62.83 ? 100 ASN B CB  1 
ATOM   3661 C CG  . ASN B 1 99  ? -11.859 47.322  32.612  1.00 67.20 ? 100 ASN B CG  1 
ATOM   3662 O OD1 . ASN B 1 99  ? -12.589 46.948  31.690  1.00 68.27 ? 100 ASN B OD1 1 
ATOM   3663 N ND2 . ASN B 1 99  ? -12.333 47.749  33.775  1.00 71.11 ? 100 ASN B ND2 1 
ATOM   3664 N N   . THR B 1 100 ? -7.722  45.853  30.387  1.00 50.00 ? 101 THR B N   1 
ATOM   3665 C CA  . THR B 1 100 ? -6.329  46.009  30.005  1.00 44.56 ? 101 THR B CA  1 
ATOM   3666 C C   . THR B 1 100 ? -6.243  46.301  28.514  1.00 40.45 ? 101 THR B C   1 
ATOM   3667 O O   . THR B 1 100 ? -7.193  46.048  27.770  1.00 41.08 ? 101 THR B O   1 
ATOM   3668 C CB  . THR B 1 100 ? -5.533  44.741  30.336  1.00 45.27 ? 101 THR B CB  1 
ATOM   3669 O OG1 . THR B 1 100 ? -5.917  43.694  29.437  1.00 43.75 ? 101 THR B OG1 1 
ATOM   3670 C CG2 . THR B 1 100 ? -5.790  44.291  31.776  1.00 47.53 ? 101 THR B CG2 1 
ATOM   3671 N N   . PRO B 1 101 ? -5.121  46.842  28.031  1.00 42.72 ? 102 PRO B N   1 
ATOM   3672 C CA  . PRO B 1 101 ? -5.054  47.199  26.600  1.00 38.69 ? 102 PRO B CA  1 
ATOM   3673 C C   . PRO B 1 101 ? -5.282  46.035  25.640  1.00 36.75 ? 102 PRO B C   1 
ATOM   3674 O O   . PRO B 1 101 ? -5.854  46.249  24.564  1.00 35.00 ? 102 PRO B O   1 
ATOM   3675 C CB  . PRO B 1 101 ? -3.647  47.791  26.462  1.00 38.10 ? 102 PRO B CB  1 
ATOM   3676 C CG  . PRO B 1 101 ? -3.395  48.408  27.807  1.00 39.42 ? 102 PRO B CG  1 
ATOM   3677 C CD  . PRO B 1 101 ? -4.001  47.428  28.793  1.00 41.37 ? 102 PRO B CD  1 
ATOM   3678 N N   . ILE B 1 102 ? -4.879  44.805  25.983  1.00 41.56 ? 103 ILE B N   1 
ATOM   3679 C CA  . ILE B 1 102 ? -5.142  43.686  25.076  1.00 35.51 ? 103 ILE B CA  1 
ATOM   3680 C C   . ILE B 1 102 ? -6.642  43.434  24.948  1.00 37.88 ? 103 ILE B C   1 
ATOM   3681 O O   . ILE B 1 102 ? -7.090  42.832  23.963  1.00 36.88 ? 103 ILE B O   1 
ATOM   3682 C CB  . ILE B 1 102 ? -4.397  42.413  25.535  1.00 36.31 ? 103 ILE B CB  1 
ATOM   3683 C CG1 . ILE B 1 102 ? -4.452  41.311  24.469  1.00 34.97 ? 103 ILE B CG1 1 
ATOM   3684 C CG2 . ILE B 1 102 ? -5.001  41.861  26.818  1.00 37.01 ? 103 ILE B CG2 1 
ATOM   3685 C CD1 . ILE B 1 102 ? -3.781  41.682  23.190  1.00 33.20 ? 103 ILE B CD1 1 
ATOM   3686 N N   . ASP B 1 103 ? -7.436  43.905  25.912  1.00 37.59 ? 104 ASP B N   1 
ATOM   3687 C CA  . ASP B 1 103 ? -8.890  43.788  25.877  1.00 39.04 ? 104 ASP B CA  1 
ATOM   3688 C C   . ASP B 1 103 ? -9.532  44.722  24.857  1.00 37.48 ? 104 ASP B C   1 
ATOM   3689 O O   . ASP B 1 103 ? -10.762 44.751  24.776  1.00 38.72 ? 104 ASP B O   1 
ATOM   3690 C CB  . ASP B 1 103 ? -9.472  44.062  27.269  1.00 40.92 ? 104 ASP B CB  1 
ATOM   3691 C CG  . ASP B 1 103 ? -10.819 43.392  27.494  1.00 44.86 ? 104 ASP B CG  1 
ATOM   3692 O OD1 . ASP B 1 103 ? -11.093 42.354  26.857  1.00 44.50 ? 104 ASP B OD1 1 
ATOM   3693 O OD2 . ASP B 1 103 ? -11.608 43.902  28.315  1.00 48.21 ? 104 ASP B OD2 1 
ATOM   3694 N N   . GLN B 1 104 ? -8.743  45.493  24.101  1.00 34.89 ? 105 GLN B N   1 
ATOM   3695 C CA  . GLN B 1 104 ? -9.231  46.258  22.961  1.00 35.57 ? 105 GLN B CA  1 
ATOM   3696 C C   . GLN B 1 104 ? -9.149  45.493  21.643  1.00 34.37 ? 105 GLN B C   1 
ATOM   3697 O O   . GLN B 1 104 ? -9.624  46.001  20.623  1.00 32.96 ? 105 GLN B O   1 
ATOM   3698 C CB  . GLN B 1 104 ? -8.448  47.565  22.828  1.00 37.48 ? 105 GLN B CB  1 
ATOM   3699 C CG  . GLN B 1 104 ? -8.622  48.511  24.008  1.00 41.43 ? 105 GLN B CG  1 
ATOM   3700 C CD  . GLN B 1 104 ? -10.072 48.901  24.204  1.00 46.11 ? 105 GLN B CD  1 
ATOM   3701 O OE1 . GLN B 1 104 ? -10.661 48.640  25.248  1.00 41.72 ? 105 GLN B OE1 1 
ATOM   3702 N NE2 . GLN B 1 104 ? -10.660 49.520  23.184  1.00 49.85 ? 105 GLN B NE2 1 
ATOM   3703 N N   . VAL B 1 105 ? -8.553  44.301  21.638  1.00 33.51 ? 106 VAL B N   1 
ATOM   3704 C CA  . VAL B 1 105 ? -8.419  43.472  20.443  1.00 32.68 ? 106 VAL B CA  1 
ATOM   3705 C C   . VAL B 1 105 ? -9.548  42.446  20.444  1.00 35.01 ? 106 VAL B C   1 
ATOM   3706 O O   . VAL B 1 105 ? -9.841  41.845  21.484  1.00 35.42 ? 106 VAL B O   1 
ATOM   3707 C CB  . VAL B 1 105 ? -7.042  42.775  20.415  1.00 34.69 ? 106 VAL B CB  1 
ATOM   3708 C CG1 . VAL B 1 105 ? -6.891  41.872  19.179  1.00 27.83 ? 106 VAL B CG1 1 
ATOM   3709 C CG2 . VAL B 1 105 ? -5.914  43.792  20.504  1.00 30.62 ? 106 VAL B CG2 1 
ATOM   3710 N N   . ASN B 1 106 ? -10.185 42.227  19.290  1.00 32.98 ? 107 ASN B N   1 
ATOM   3711 C CA  . ASN B 1 106 ? -11.256 41.238  19.285  1.00 32.38 ? 107 ASN B CA  1 
ATOM   3712 C C   . ASN B 1 106 ? -10.735 39.867  18.848  1.00 31.56 ? 107 ASN B C   1 
ATOM   3713 O O   . ASN B 1 106 ? -9.613  39.724  18.365  1.00 31.45 ? 107 ASN B O   1 
ATOM   3714 C CB  . ASN B 1 106 ? -12.444 41.696  18.425  1.00 32.60 ? 107 ASN B CB  1 
ATOM   3715 C CG  . ASN B 1 106 ? -12.164 41.690  16.929  1.00 32.05 ? 107 ASN B CG  1 
ATOM   3716 O OD1 . ASN B 1 106 ? -11.477 40.813  16.389  1.00 32.54 ? 107 ASN B OD1 1 
ATOM   3717 N ND2 . ASN B 1 106 ? -12.742 42.664  16.242  1.00 29.27 ? 107 ASN B ND2 1 
ATOM   3718 N N   . LEU B 1 107 ? -11.582 38.849  19.033  1.00 28.51 ? 108 LEU B N   1 
ATOM   3719 C CA  . LEU B 1 107 ? -11.151 37.463  18.835  1.00 30.82 ? 108 LEU B CA  1 
ATOM   3720 C C   . LEU B 1 107 ? -10.757 37.188  17.388  1.00 29.43 ? 108 LEU B C   1 
ATOM   3721 O O   . LEU B 1 107 ? -9.811  36.433  17.128  1.00 31.11 ? 108 LEU B O   1 
ATOM   3722 C CB  . LEU B 1 107 ? -12.260 36.509  19.270  1.00 32.02 ? 108 LEU B CB  1 
ATOM   3723 C CG  . LEU B 1 107 ? -12.746 36.688  20.707  1.00 35.34 ? 108 LEU B CG  1 
ATOM   3724 C CD1 . LEU B 1 107 ? -13.776 35.629  21.057  1.00 37.34 ? 108 LEU B CD1 1 
ATOM   3725 C CD2 . LEU B 1 107 ? -11.571 36.654  21.672  1.00 37.79 ? 108 LEU B CD2 1 
ATOM   3726 N N   . LEU B 1 108 ? -11.470 37.779  16.429  1.00 27.86 ? 109 LEU B N   1 
ATOM   3727 C CA  . LEU B 1 108 ? -11.106 37.571  15.029  1.00 27.93 ? 109 LEU B CA  1 
ATOM   3728 C C   . LEU B 1 108 ? -9.719  38.133  14.738  1.00 26.51 ? 109 LEU B C   1 
ATOM   3729 O O   . LEU B 1 108 ? -8.944  37.539  13.976  1.00 25.20 ? 109 LEU B O   1 
ATOM   3730 C CB  . LEU B 1 108 ? -12.153 38.210  14.111  1.00 29.98 ? 109 LEU B CB  1 
ATOM   3731 C CG  . LEU B 1 108 ? -11.862 38.066  12.612  1.00 31.42 ? 109 LEU B CG  1 
ATOM   3732 C CD1 . LEU B 1 108 ? -11.800 36.609  12.212  1.00 29.94 ? 109 LEU B CD1 1 
ATOM   3733 C CD2 . LEU B 1 108 ? -12.905 38.792  11.774  1.00 37.76 ? 109 LEU B CD2 1 
ATOM   3734 N N   . GLN B 1 109 ? -9.388  39.278  15.340  1.00 26.01 ? 110 GLN B N   1 
ATOM   3735 C CA  . GLN B 1 109 ? -8.078  39.880  15.123  1.00 24.68 ? 110 GLN B CA  1 
ATOM   3736 C C   . GLN B 1 109 ? -6.969  39.043  15.747  1.00 21.63 ? 110 GLN B C   1 
ATOM   3737 O O   . GLN B 1 109 ? -5.876  38.935  15.177  1.00 23.03 ? 110 GLN B O   1 
ATOM   3738 C CB  . GLN B 1 109 ? -8.075  41.318  15.668  1.00 22.84 ? 110 GLN B CB  1 
ATOM   3739 C CG  . GLN B 1 109 ? -9.015  42.207  14.867  1.00 22.38 ? 110 GLN B CG  1 
ATOM   3740 C CD  . GLN B 1 109 ? -9.342  43.521  15.537  1.00 29.56 ? 110 GLN B CD  1 
ATOM   3741 O OE1 . GLN B 1 109 ? -9.399  43.610  16.764  1.00 27.60 ? 110 GLN B OE1 1 
ATOM   3742 N NE2 . GLN B 1 109 ? -9.573  44.556  14.729  1.00 26.67 ? 110 GLN B NE2 1 
ATOM   3743 N N   . LEU B 1 110 ? -7.216  38.456  16.925  1.00 22.07 ? 111 LEU B N   1 
ATOM   3744 C CA  . LEU B 1 110 ? -6.246  37.520  17.489  1.00 28.01 ? 111 LEU B CA  1 
ATOM   3745 C C   . LEU B 1 110 ? -6.066  36.303  16.588  1.00 24.40 ? 111 LEU B C   1 
ATOM   3746 O O   . LEU B 1 110 ? -4.935  35.871  16.332  1.00 25.11 ? 111 LEU B O   1 
ATOM   3747 C CB  . LEU B 1 110 ? -6.681  37.083  18.893  1.00 26.14 ? 111 LEU B CB  1 
ATOM   3748 C CG  . LEU B 1 110 ? -6.751  38.183  19.961  1.00 25.87 ? 111 LEU B CG  1 
ATOM   3749 C CD1 . LEU B 1 110 ? -7.510  37.654  21.171  1.00 30.61 ? 111 LEU B CD1 1 
ATOM   3750 C CD2 . LEU B 1 110 ? -5.358  38.660  20.366  1.00 24.57 ? 111 LEU B CD2 1 
ATOM   3751 N N   . ALA B 1 111 ? -7.170  35.752  16.080  1.00 23.80 ? 112 ALA B N   1 
ATOM   3752 C CA  . ALA B 1 111 ? -7.105  34.518  15.297  1.00 24.42 ? 112 ALA B CA  1 
ATOM   3753 C C   . ALA B 1 111 ? -6.422  34.718  13.949  1.00 25.35 ? 112 ALA B C   1 
ATOM   3754 O O   . ALA B 1 111 ? -5.904  33.751  13.381  1.00 23.38 ? 112 ALA B O   1 
ATOM   3755 C CB  . ALA B 1 111 ? -8.511  33.965  15.081  1.00 24.89 ? 112 ALA B CB  1 
ATOM   3756 N N   . THR B 1 112 ? -6.426  35.942  13.418  1.00 22.19 ? 113 THR B N   1 
ATOM   3757 C CA  . THR B 1 112 ? -5.856  36.233  12.105  1.00 21.56 ? 113 THR B CA  1 
ATOM   3758 C C   . THR B 1 112 ? -4.685  37.216  12.201  1.00 21.48 ? 113 THR B C   1 
ATOM   3759 O O   . THR B 1 112 ? -4.316  37.859  11.204  1.00 19.58 ? 113 THR B O   1 
ATOM   3760 C CB  . THR B 1 112 ? -6.937  36.766  11.157  1.00 25.16 ? 113 THR B CB  1 
ATOM   3761 O OG1 . THR B 1 112 ? -7.469  37.993  11.679  1.00 21.98 ? 113 THR B OG1 1 
ATOM   3762 C CG2 . THR B 1 112 ? -8.070  35.753  11.000  1.00 21.60 ? 113 THR B CG2 1 
ATOM   3763 N N   . TYR B 1 113 ? -4.104  37.348  13.397  1.00 19.87 ? 114 TYR B N   1 
ATOM   3764 C CA  . TYR B 1 113 ? -2.752  37.867  13.596  1.00 20.95 ? 114 TYR B CA  1 
ATOM   3765 C C   . TYR B 1 113 ? -2.659  39.388  13.418  1.00 20.77 ? 114 TYR B C   1 
ATOM   3766 O O   . TYR B 1 113 ? -1.612  39.887  13.023  1.00 20.33 ? 114 TYR B O   1 
ATOM   3767 C CB  . TYR B 1 113 ? -1.740  37.192  12.657  1.00 21.05 ? 114 TYR B CB  1 
ATOM   3768 C CG  . TYR B 1 113 ? -1.930  35.692  12.458  1.00 18.82 ? 114 TYR B CG  1 
ATOM   3769 C CD1 . TYR B 1 113 ? -1.814  34.812  13.518  1.00 22.08 ? 114 TYR B CD1 1 
ATOM   3770 C CD2 . TYR B 1 113 ? -2.212  35.172  11.196  1.00 18.92 ? 114 TYR B CD2 1 
ATOM   3771 C CE1 . TYR B 1 113 ? -1.983  33.430  13.328  1.00 21.99 ? 114 TYR B CE1 1 
ATOM   3772 C CE2 . TYR B 1 113 ? -2.386  33.805  10.996  1.00 21.96 ? 114 TYR B CE2 1 
ATOM   3773 C CZ  . TYR B 1 113 ? -2.267  32.938  12.060  1.00 22.67 ? 114 TYR B CZ  1 
ATOM   3774 O OH  . TYR B 1 113 ? -2.442  31.576  11.849  1.00 29.14 ? 114 TYR B OH  1 
ATOM   3775 N N   . THR B 1 114 ? -3.720  40.142  13.710  1.00 20.82 ? 115 THR B N   1 
ATOM   3776 C CA  . THR B 1 114 ? -3.704  41.582  13.451  1.00 19.71 ? 115 THR B CA  1 
ATOM   3777 C C   . THR B 1 114 ? -3.825  42.426  14.719  1.00 24.05 ? 115 THR B C   1 
ATOM   3778 O O   . THR B 1 114 ? -4.229  43.590  14.650  1.00 23.08 ? 115 THR B O   1 
ATOM   3779 C CB  . THR B 1 114 ? -4.785  42.000  12.445  1.00 23.47 ? 115 THR B CB  1 
ATOM   3780 O OG1 . THR B 1 114 ? -6.088  41.682  12.949  1.00 24.41 ? 115 THR B OG1 1 
ATOM   3781 C CG2 . THR B 1 114 ? -4.576  41.330  11.084  1.00 23.08 ? 115 THR B CG2 1 
ATOM   3782 N N   . SER B 1 115 ? -3.402  41.898  15.875  1.00 19.80 ? 116 SER B N   1 
ATOM   3783 C CA  . SER B 1 115 ? -3.416  42.717  17.092  1.00 22.59 ? 116 SER B CA  1 
ATOM   3784 C C   . SER B 1 115 ? -2.547  43.962  16.960  1.00 23.63 ? 116 SER B C   1 
ATOM   3785 O O   . SER B 1 115 ? -2.792  44.964  17.646  1.00 22.88 ? 116 SER B O   1 
ATOM   3786 C CB  . SER B 1 115 ? -2.938  41.906  18.292  1.00 23.77 ? 116 SER B CB  1 
ATOM   3787 O OG  . SER B 1 115 ? -1.522  41.809  18.253  1.00 23.68 ? 116 SER B OG  1 
ATOM   3788 N N   . GLY B 1 116 ? -1.500  43.905  16.136  1.00 21.51 ? 117 GLY B N   1 
ATOM   3789 C CA  . GLY B 1 116 ? -0.604  45.028  15.946  1.00 22.63 ? 117 GLY B CA  1 
ATOM   3790 C C   . GLY B 1 116 ? 0.653   44.989  16.794  1.00 23.48 ? 117 GLY B C   1 
ATOM   3791 O O   . GLY B 1 116 ? 1.546   45.817  16.581  1.00 26.68 ? 117 GLY B O   1 
ATOM   3792 N N   . ASN B 1 117 ? 0.757   44.058  17.749  1.00 21.50 ? 118 ASN B N   1 
ATOM   3793 C CA  . ASN B 1 117 ? 1.990   43.957  18.528  1.00 23.14 ? 118 ASN B CA  1 
ATOM   3794 C C   . ASN B 1 117 ? 2.157   42.572  19.160  1.00 24.39 ? 118 ASN B C   1 
ATOM   3795 O O   . ASN B 1 117 ? 2.299   42.455  20.383  1.00 25.05 ? 118 ASN B O   1 
ATOM   3796 C CB  . ASN B 1 117 ? 2.025   45.044  19.610  1.00 23.35 ? 118 ASN B CB  1 
ATOM   3797 C CG  . ASN B 1 117 ? 3.408   45.209  20.239  1.00 24.16 ? 118 ASN B CG  1 
ATOM   3798 O OD1 . ASN B 1 117 ? 4.422   44.938  19.610  1.00 26.32 ? 118 ASN B OD1 1 
ATOM   3799 N ND2 . ASN B 1 117 ? 3.444   45.642  21.483  1.00 28.05 ? 118 ASN B ND2 1 
ATOM   3800 N N   . LEU B 1 118 ? 2.137   41.522  18.342  1.00 24.61 ? 119 LEU B N   1 
ATOM   3801 C CA  . LEU B 1 118 ? 2.424   40.160  18.804  1.00 26.51 ? 119 LEU B CA  1 
ATOM   3802 C C   . LEU B 1 118 ? 3.318   39.499  17.767  1.00 26.57 ? 119 LEU B C   1 
ATOM   3803 O O   . LEU B 1 118 ? 2.959   39.426  16.586  1.00 24.42 ? 119 LEU B O   1 
ATOM   3804 C CB  . LEU B 1 118 ? 1.146   39.344  19.039  1.00 24.44 ? 119 LEU B CB  1 
ATOM   3805 C CG  . LEU B 1 118 ? 0.322   39.778  20.264  1.00 26.21 ? 119 LEU B CG  1 
ATOM   3806 C CD1 . LEU B 1 118 ? -1.030  39.064  20.327  1.00 26.13 ? 119 LEU B CD1 1 
ATOM   3807 C CD2 . LEU B 1 118 ? 1.108   39.546  21.576  1.00 29.39 ? 119 LEU B CD2 1 
ATOM   3808 N N   . ALA B 1 119 ? 4.500   39.079  18.205  1.00 26.58 ? 120 ALA B N   1 
ATOM   3809 C CA  . ALA B 1 119 ? 5.532   38.520  17.346  1.00 26.98 ? 120 ALA B CA  1 
ATOM   3810 C C   . ALA B 1 119 ? 5.327   37.019  17.152  1.00 27.62 ? 120 ALA B C   1 
ATOM   3811 O O   . ALA B 1 119 ? 4.356   36.430  17.633  1.00 27.72 ? 120 ALA B O   1 
ATOM   3812 C CB  . ALA B 1 119 ? 6.914   38.789  17.944  1.00 31.05 ? 120 ALA B CB  1 
ATOM   3813 N N   . LEU B 1 120 ? 6.273   36.388  16.446  1.00 27.34 ? 121 LEU B N   1 
ATOM   3814 C CA  . LEU B 1 120 ? 6.129   34.968  16.114  1.00 27.53 ? 121 LEU B CA  1 
ATOM   3815 C C   . LEU B 1 120 ? 6.048   34.103  17.368  1.00 28.39 ? 121 LEU B C   1 
ATOM   3816 O O   . LEU B 1 120 ? 5.201   33.205  17.453  1.00 29.32 ? 121 LEU B O   1 
ATOM   3817 C CB  . LEU B 1 120 ? 7.285   34.516  15.218  1.00 29.39 ? 121 LEU B CB  1 
ATOM   3818 C CG  . LEU B 1 120 ? 7.316   33.030  14.841  1.00 34.66 ? 121 LEU B CG  1 
ATOM   3819 C CD1 . LEU B 1 120 ? 6.108   32.637  13.976  1.00 28.77 ? 121 LEU B CD1 1 
ATOM   3820 C CD2 . LEU B 1 120 ? 8.624   32.690  14.137  1.00 36.17 ? 121 LEU B CD2 1 
ATOM   3821 N N   . GLN B 1 121 ? 6.910   34.355  18.352  1.00 30.97 ? 122 GLN B N   1 
ATOM   3822 C CA  . GLN B 1 121 ? 6.921   33.604  19.600  1.00 33.06 ? 122 GLN B CA  1 
ATOM   3823 C C   . GLN B 1 121 ? 6.749   34.542  20.788  1.00 35.05 ? 122 GLN B C   1 
ATOM   3824 O O   . GLN B 1 121 ? 6.952   35.755  20.682  1.00 32.67 ? 122 GLN B O   1 
ATOM   3825 C CB  . GLN B 1 121 ? 8.233   32.812  19.788  1.00 33.34 ? 122 GLN B CB  1 
ATOM   3826 C CG  . GLN B 1 121 ? 8.670   31.967  18.597  1.00 33.45 ? 122 GLN B CG  1 
ATOM   3827 C CD  . GLN B 1 121 ? 7.771   30.766  18.351  1.00 33.74 ? 122 GLN B CD  1 
ATOM   3828 O OE1 . GLN B 1 121 ? 6.939   30.410  19.187  1.00 34.54 ? 122 GLN B OE1 1 
ATOM   3829 N NE2 . GLN B 1 121 ? 7.930   30.142  17.193  1.00 35.48 ? 122 GLN B NE2 1 
ATOM   3830 N N   . PHE B 1 122 ? 6.379   33.956  21.933  1.00 33.79 ? 123 PHE B N   1 
ATOM   3831 C CA  . PHE B 1 122 ? 6.495   34.654  23.208  1.00 40.71 ? 123 PHE B CA  1 
ATOM   3832 C C   . PHE B 1 122 ? 7.949   35.057  23.448  1.00 43.92 ? 123 PHE B C   1 
ATOM   3833 O O   . PHE B 1 122 ? 8.865   34.497  22.841  1.00 39.79 ? 123 PHE B O   1 
ATOM   3834 C CB  . PHE B 1 122 ? 6.034   33.763  24.365  1.00 39.77 ? 123 PHE B CB  1 
ATOM   3835 C CG  . PHE B 1 122 ? 4.540   33.658  24.517  1.00 39.91 ? 123 PHE B CG  1 
ATOM   3836 C CD1 . PHE B 1 122 ? 3.822   34.652  25.172  1.00 37.48 ? 123 PHE B CD1 1 
ATOM   3837 C CD2 . PHE B 1 122 ? 3.855   32.554  24.024  1.00 38.88 ? 123 PHE B CD2 1 
ATOM   3838 C CE1 . PHE B 1 122 ? 2.444   34.549  25.332  1.00 35.63 ? 123 PHE B CE1 1 
ATOM   3839 C CE2 . PHE B 1 122 ? 2.477   32.441  24.176  1.00 35.94 ? 123 PHE B CE2 1 
ATOM   3840 C CZ  . PHE B 1 122 ? 1.771   33.434  24.835  1.00 39.16 ? 123 PHE B CZ  1 
ATOM   3841 N N   . PRO B 1 123 ? 8.188   36.021  24.337  1.00 44.79 ? 124 PRO B N   1 
ATOM   3842 C CA  . PRO B 1 123 ? 9.559   36.240  24.816  1.00 49.38 ? 124 PRO B CA  1 
ATOM   3843 C C   . PRO B 1 123 ? 10.103  34.975  25.465  1.00 50.45 ? 124 PRO B C   1 
ATOM   3844 O O   . PRO B 1 123 ? 9.354   34.163  26.014  1.00 47.58 ? 124 PRO B O   1 
ATOM   3845 C CB  . PRO B 1 123 ? 9.408   37.378  25.835  1.00 51.28 ? 124 PRO B CB  1 
ATOM   3846 C CG  . PRO B 1 123 ? 8.160   38.089  25.425  1.00 47.46 ? 124 PRO B CG  1 
ATOM   3847 C CD  . PRO B 1 123 ? 7.247   37.020  24.865  1.00 45.55 ? 124 PRO B CD  1 
ATOM   3848 N N   . ASP B 1 124 ? 11.416  34.778  25.370  1.00 52.82 ? 125 ASP B N   1 
ATOM   3849 C CA  . ASP B 1 124 ? 12.021  33.530  25.909  1.00 54.16 ? 125 ASP B CA  1 
ATOM   3850 C C   . ASP B 1 124 ? 11.751  33.405  27.413  1.00 53.78 ? 125 ASP B C   1 
ATOM   3851 O O   . ASP B 1 124 ? 11.620  32.271  27.879  1.00 55.59 ? 125 ASP B O   1 
ATOM   3852 C CB  . ASP B 1 124 ? 13.509  33.429  25.586  1.00 57.50 ? 125 ASP B CB  1 
ATOM   3853 C CG  . ASP B 1 124 ? 13.864  33.975  24.216  1.00 65.89 ? 125 ASP B CG  1 
ATOM   3854 O OD1 . ASP B 1 124 ? 14.091  35.192  24.120  1.00 67.89 ? 125 ASP B OD1 1 
ATOM   3855 O OD2 . ASP B 1 124 ? 13.906  33.178  23.261  1.00 67.07 ? 125 ASP B OD2 1 
ATOM   3856 N N   . GLU B 1 125 ? 11.662  34.519  28.134  1.00 52.68 ? 126 GLU B N   1 
ATOM   3857 C CA  . GLU B 1 125 ? 11.446  34.436  29.575  1.00 56.77 ? 126 GLU B CA  1 
ATOM   3858 C C   . GLU B 1 125 ? 10.017  34.063  29.941  1.00 54.39 ? 126 GLU B C   1 
ATOM   3859 O O   . GLU B 1 125 ? 9.738   33.836  31.122  1.00 55.20 ? 126 GLU B O   1 
ATOM   3860 C CB  . GLU B 1 125 ? 11.812  35.765  30.244  1.00 57.67 ? 126 GLU B CB  1 
ATOM   3861 C CG  . GLU B 1 125 ? 10.953  36.945  29.809  1.00 61.22 ? 126 GLU B CG  1 
ATOM   3862 C CD  . GLU B 1 125 ? 11.583  37.768  28.693  1.00 61.40 ? 126 GLU B CD  1 
ATOM   3863 O OE1 . GLU B 1 125 ? 11.355  38.999  28.663  1.00 65.07 ? 126 GLU B OE1 1 
ATOM   3864 O OE2 . GLU B 1 125 ? 12.304  37.188  27.849  1.00 61.09 ? 126 GLU B OE2 1 
ATOM   3865 N N   . VAL B 1 126 ? 9.117   33.981  28.965  1.00 53.04 ? 127 VAL B N   1 
ATOM   3866 C CA  . VAL B 1 126 ? 7.706   33.703  29.213  1.00 53.59 ? 127 VAL B CA  1 
ATOM   3867 C C   . VAL B 1 126 ? 7.510   32.190  29.136  1.00 52.65 ? 127 VAL B C   1 
ATOM   3868 O O   . VAL B 1 126 ? 7.463   31.608  28.049  1.00 50.19 ? 127 VAL B O   1 
ATOM   3869 C CB  . VAL B 1 126 ? 6.812   34.454  28.222  1.00 46.64 ? 127 VAL B CB  1 
ATOM   3870 C CG1 . VAL B 1 126 ? 5.354   34.076  28.422  1.00 49.75 ? 127 VAL B CG1 1 
ATOM   3871 C CG2 . VAL B 1 126 ? 7.006   35.958  28.383  1.00 49.26 ? 127 VAL B CG2 1 
ATOM   3872 N N   . LYS B 1 127 ? 7.381   31.547  30.301  1.00 53.43 ? 128 LYS B N   1 
ATOM   3873 C CA  . LYS B 1 127 ? 7.272   30.091  30.362  1.00 51.96 ? 128 LYS B CA  1 
ATOM   3874 C C   . LYS B 1 127 ? 6.041   29.630  31.138  1.00 51.81 ? 128 LYS B C   1 
ATOM   3875 O O   . LYS B 1 127 ? 5.177   28.941  30.586  1.00 51.73 ? 128 LYS B O   1 
ATOM   3876 C CB  . LYS B 1 127 ? 8.536   29.495  30.986  1.00 54.03 ? 128 LYS B CB  1 
ATOM   3877 C CG  . LYS B 1 127 ? 9.808   29.816  30.213  1.00 60.48 ? 128 LYS B CG  1 
ATOM   3878 C CD  . LYS B 1 127 ? 11.063  29.424  30.982  1.00 63.75 ? 128 LYS B CD  1 
ATOM   3879 C CE  . LYS B 1 127 ? 12.309  29.588  30.119  1.00 63.56 ? 128 LYS B CE  1 
ATOM   3880 N NZ  . LYS B 1 127 ? 12.248  28.728  28.902  1.00 65.19 ? 128 LYS B NZ  1 
ATOM   3881 N N   . THR B 1 128 ? 5.953   30.009  32.412  1.00 51.69 ? 129 THR B N   1 
ATOM   3882 C CA  . THR B 1 128 ? 4.896   29.544  33.302  1.00 54.22 ? 129 THR B CA  1 
ATOM   3883 C C   . THR B 1 128 ? 3.543   30.136  32.904  1.00 52.88 ? 129 THR B C   1 
ATOM   3884 O O   . THR B 1 128 ? 3.446   31.035  32.065  1.00 55.60 ? 129 THR B O   1 
ATOM   3885 C CB  . THR B 1 128 ? 5.220   29.913  34.751  1.00 55.89 ? 129 THR B CB  1 
ATOM   3886 O OG1 . THR B 1 128 ? 4.814   31.267  35.011  1.00 56.38 ? 129 THR B OG1 1 
ATOM   3887 C CG2 . THR B 1 128 ? 6.714   29.805  34.993  1.00 57.41 ? 129 THR B CG2 1 
ATOM   3888 N N   . ASP B 1 129 ? 2.486   29.621  33.537  1.00 53.23 ? 130 ASP B N   1 
ATOM   3889 C CA  . ASP B 1 129 ? 1.145   30.146  33.299  1.00 56.30 ? 130 ASP B CA  1 
ATOM   3890 C C   . ASP B 1 129 ? 1.024   31.580  33.792  1.00 55.00 ? 130 ASP B C   1 
ATOM   3891 O O   . ASP B 1 129 ? 0.502   32.449  33.084  1.00 53.48 ? 130 ASP B O   1 
ATOM   3892 C CB  . ASP B 1 129 ? 0.097   29.273  33.985  1.00 53.08 ? 130 ASP B CB  1 
ATOM   3893 C CG  . ASP B 1 129 ? 0.106   27.850  33.488  1.00 57.94 ? 130 ASP B CG  1 
ATOM   3894 O OD1 . ASP B 1 129 ? 0.143   27.642  32.254  1.00 56.41 ? 130 ASP B OD1 1 
ATOM   3895 O OD2 . ASP B 1 129 ? 0.080   26.937  34.342  1.00 60.70 ? 130 ASP B OD2 1 
ATOM   3896 N N   . GLN B 1 130 ? 1.485   31.844  35.017  1.00 56.29 ? 131 GLN B N   1 
ATOM   3897 C CA  . GLN B 1 130 ? 1.413   33.202  35.544  1.00 53.42 ? 131 GLN B CA  1 
ATOM   3898 C C   . GLN B 1 130 ? 2.239   34.172  34.711  1.00 53.31 ? 131 GLN B C   1 
ATOM   3899 O O   . GLN B 1 130 ? 1.851   35.334  34.546  1.00 52.68 ? 131 GLN B O   1 
ATOM   3900 C CB  . GLN B 1 130 ? 1.865   33.223  37.002  1.00 62.65 ? 131 GLN B CB  1 
ATOM   3901 C CG  . GLN B 1 130 ? 0.794   32.736  37.977  1.00 65.75 ? 131 GLN B CG  1 
ATOM   3902 C CD  . GLN B 1 130 ? -0.534  33.462  37.790  1.00 64.29 ? 131 GLN B CD  1 
ATOM   3903 O OE1 . GLN B 1 130 ? -0.678  34.639  38.155  1.00 58.33 ? 131 GLN B OE1 1 
ATOM   3904 N NE2 . GLN B 1 130 ? -1.508  32.765  37.200  1.00 59.46 ? 131 GLN B NE2 1 
ATOM   3905 N N   . GLN B 1 131 ? 3.368   33.718  34.164  1.00 53.94 ? 132 GLN B N   1 
ATOM   3906 C CA  . GLN B 1 131 ? 4.148   34.587  33.289  1.00 54.23 ? 132 GLN B CA  1 
ATOM   3907 C C   . GLN B 1 131 ? 3.382   34.920  32.013  1.00 50.59 ? 132 GLN B C   1 
ATOM   3908 O O   . GLN B 1 131 ? 3.467   36.047  31.511  1.00 46.60 ? 132 GLN B O   1 
ATOM   3909 C CB  . GLN B 1 131 ? 5.493   33.940  32.967  1.00 52.49 ? 132 GLN B CB  1 
ATOM   3910 C CG  . GLN B 1 131 ? 6.455   33.928  34.147  1.00 53.34 ? 132 GLN B CG  1 
ATOM   3911 C CD  . GLN B 1 131 ? 7.734   33.179  33.843  1.00 57.47 ? 132 GLN B CD  1 
ATOM   3912 O OE1 . GLN B 1 131 ? 7.740   32.225  33.061  1.00 56.16 ? 132 GLN B OE1 1 
ATOM   3913 N NE2 . GLN B 1 131 ? 8.828   33.608  34.455  1.00 58.28 ? 132 GLN B NE2 1 
ATOM   3914 N N   . VAL B 1 132 ? 2.628   33.955  31.474  1.00 50.40 ? 133 VAL B N   1 
ATOM   3915 C CA  . VAL B 1 132 ? 1.774   34.237  30.320  1.00 49.34 ? 133 VAL B CA  1 
ATOM   3916 C C   . VAL B 1 132 ? 0.768   35.330  30.658  1.00 48.96 ? 133 VAL B C   1 
ATOM   3917 O O   . VAL B 1 132 ? 0.584   36.292  29.899  1.00 44.32 ? 133 VAL B O   1 
ATOM   3918 C CB  . VAL B 1 132 ? 1.056   32.962  29.849  1.00 49.08 ? 133 VAL B CB  1 
ATOM   3919 C CG1 . VAL B 1 132 ? -0.038  33.330  28.845  1.00 40.32 ? 133 VAL B CG1 1 
ATOM   3920 C CG2 . VAL B 1 132 ? 2.043   31.997  29.233  1.00 50.70 ? 133 VAL B CG2 1 
ATOM   3921 N N   . LEU B 1 133 ? 0.099   35.191  31.805  1.00 47.85 ? 134 LEU B N   1 
ATOM   3922 C CA  . LEU B 1 133 ? -0.895  36.179  32.210  1.00 50.54 ? 134 LEU B CA  1 
ATOM   3923 C C   . LEU B 1 133 ? -0.266  37.558  32.404  1.00 46.54 ? 134 LEU B C   1 
ATOM   3924 O O   . LEU B 1 133 ? -0.825  38.566  31.956  1.00 45.49 ? 134 LEU B O   1 
ATOM   3925 C CB  . LEU B 1 133 ? -1.602  35.707  33.485  1.00 50.75 ? 134 LEU B CB  1 
ATOM   3926 C CG  . LEU B 1 133 ? -2.668  36.630  34.080  1.00 51.21 ? 134 LEU B CG  1 
ATOM   3927 C CD1 . LEU B 1 133 ? -3.680  37.018  33.020  1.00 48.23 ? 134 LEU B CD1 1 
ATOM   3928 C CD2 . LEU B 1 133 ? -3.358  35.947  35.247  1.00 54.73 ? 134 LEU B CD2 1 
ATOM   3929 N N   . THR B 1 134 ? 0.901   37.621  33.062  1.00 45.81 ? 135 THR B N   1 
ATOM   3930 C CA  . THR B 1 134 ? 1.589   38.899  33.246  1.00 47.79 ? 135 THR B CA  1 
ATOM   3931 C C   . THR B 1 134 ? 1.968   39.518  31.904  1.00 43.69 ? 135 THR B C   1 
ATOM   3932 O O   . THR B 1 134 ? 1.800   40.724  31.701  1.00 43.51 ? 135 THR B O   1 
ATOM   3933 C CB  . THR B 1 134 ? 2.837   38.716  34.120  1.00 48.18 ? 135 THR B CB  1 
ATOM   3934 O OG1 . THR B 1 134 ? 2.458   38.503  35.487  1.00 50.36 ? 135 THR B OG1 1 
ATOM   3935 C CG2 . THR B 1 134 ? 3.746   39.948  34.043  1.00 45.62 ? 135 THR B CG2 1 
ATOM   3936 N N   . PHE B 1 135 ? 2.488   38.706  30.979  1.00 44.34 ? 136 PHE B N   1 
ATOM   3937 C CA  . PHE B 1 135 ? 2.804   39.195  29.638  1.00 40.12 ? 136 PHE B CA  1 
ATOM   3938 C C   . PHE B 1 135 ? 1.607   39.885  28.991  1.00 41.44 ? 136 PHE B C   1 
ATOM   3939 O O   . PHE B 1 135 ? 1.745   40.969  28.406  1.00 40.72 ? 136 PHE B O   1 
ATOM   3940 C CB  . PHE B 1 135 ? 3.287   38.036  28.759  1.00 41.24 ? 136 PHE B CB  1 
ATOM   3941 C CG  . PHE B 1 135 ? 3.486   38.405  27.312  1.00 41.87 ? 136 PHE B CG  1 
ATOM   3942 C CD1 . PHE B 1 135 ? 4.653   39.025  26.893  1.00 41.54 ? 136 PHE B CD1 1 
ATOM   3943 C CD2 . PHE B 1 135 ? 2.513   38.109  26.366  1.00 39.74 ? 136 PHE B CD2 1 
ATOM   3944 C CE1 . PHE B 1 135 ? 4.835   39.357  25.561  1.00 40.80 ? 136 PHE B CE1 1 
ATOM   3945 C CE2 . PHE B 1 135 ? 2.692   38.440  25.028  1.00 35.01 ? 136 PHE B CE2 1 
ATOM   3946 C CZ  . PHE B 1 135 ? 3.854   39.060  24.628  1.00 36.18 ? 136 PHE B CZ  1 
ATOM   3947 N N   . PHE B 1 136 ? 0.419   39.283  29.092  1.00 39.20 ? 137 PHE B N   1 
ATOM   3948 C CA  . PHE B 1 136 ? -0.739  39.889  28.443  1.00 38.68 ? 137 PHE B CA  1 
ATOM   3949 C C   . PHE B 1 136 ? -1.301  41.077  29.221  1.00 38.64 ? 137 PHE B C   1 
ATOM   3950 O O   . PHE B 1 136 ? -1.834  42.004  28.606  1.00 36.27 ? 137 PHE B O   1 
ATOM   3951 C CB  . PHE B 1 136 ? -1.825  38.841  28.203  1.00 37.79 ? 137 PHE B CB  1 
ATOM   3952 C CG  . PHE B 1 136 ? -1.568  37.968  26.996  1.00 38.45 ? 137 PHE B CG  1 
ATOM   3953 C CD1 . PHE B 1 136 ? -1.496  38.521  25.725  1.00 35.59 ? 137 PHE B CD1 1 
ATOM   3954 C CD2 . PHE B 1 136 ? -1.408  36.592  27.129  1.00 38.82 ? 137 PHE B CD2 1 
ATOM   3955 C CE1 . PHE B 1 136 ? -1.263  37.718  24.614  1.00 34.04 ? 137 PHE B CE1 1 
ATOM   3956 C CE2 . PHE B 1 136 ? -1.177  35.787  26.013  1.00 37.61 ? 137 PHE B CE2 1 
ATOM   3957 C CZ  . PHE B 1 136 ? -1.103  36.359  24.761  1.00 32.01 ? 137 PHE B CZ  1 
ATOM   3958 N N   . LYS B 1 137 ? -1.200  41.077  30.554  1.00 38.74 ? 138 LYS B N   1 
ATOM   3959 C CA  . LYS B 1 137 ? -1.606  42.263  31.314  1.00 40.30 ? 138 LYS B CA  1 
ATOM   3960 C C   . LYS B 1 137 ? -0.709  43.460  31.024  1.00 41.89 ? 138 LYS B C   1 
ATOM   3961 O O   . LYS B 1 137 ? -1.176  44.609  31.062  1.00 40.13 ? 138 LYS B O   1 
ATOM   3962 C CB  . LYS B 1 137 ? -1.589  41.980  32.815  1.00 43.06 ? 138 LYS B CB  1 
ATOM   3963 C CG  . LYS B 1 137 ? -2.714  41.093  33.323  1.00 49.45 ? 138 LYS B CG  1 
ATOM   3964 C CD  . LYS B 1 137 ? -2.666  41.017  34.857  1.00 52.89 ? 138 LYS B CD  1 
ATOM   3965 C CE  . LYS B 1 137 ? -3.768  40.143  35.423  1.00 52.66 ? 138 LYS B CE  1 
ATOM   3966 N NZ  . LYS B 1 137 ? -4.043  40.492  36.847  1.00 57.37 ? 138 LYS B NZ  1 
ATOM   3967 N N   . ASP B 1 138 ? 0.579   43.224  30.763  1.00 39.25 ? 139 ASP B N   1 
ATOM   3968 C CA  . ASP B 1 138 ? 1.511   44.316  30.508  1.00 41.42 ? 139 ASP B CA  1 
ATOM   3969 C C   . ASP B 1 138 ? 1.553   44.726  29.041  1.00 38.81 ? 139 ASP B C   1 
ATOM   3970 O O   . ASP B 1 138 ? 2.184   45.741  28.718  1.00 41.35 ? 139 ASP B O   1 
ATOM   3971 C CB  . ASP B 1 138 ? 2.926   43.940  30.964  1.00 40.62 ? 139 ASP B CB  1 
ATOM   3972 C CG  . ASP B 1 138 ? 2.997   43.602  32.440  1.00 46.03 ? 139 ASP B CG  1 
ATOM   3973 O OD1 . ASP B 1 138 ? 2.095   44.019  33.199  1.00 46.91 ? 139 ASP B OD1 1 
ATOM   3974 O OD2 . ASP B 1 138 ? 3.962   42.919  32.842  1.00 48.58 ? 139 ASP B OD2 1 
ATOM   3975 N N   . TRP B 1 139 ? 0.882   43.975  28.168  1.00 37.56 ? 140 TRP B N   1 
ATOM   3976 C CA  . TRP B 1 139 ? 0.866   44.259  26.734  1.00 37.90 ? 140 TRP B CA  1 
ATOM   3977 C C   . TRP B 1 139 ? 0.316   45.650  26.442  1.00 36.40 ? 140 TRP B C   1 
ATOM   3978 O O   . TRP B 1 139 ? -0.633  46.113  27.079  1.00 35.32 ? 140 TRP B O   1 
ATOM   3979 C CB  . TRP B 1 139 ? 0.022   43.200  26.021  1.00 32.63 ? 140 TRP B CB  1 
ATOM   3980 C CG  . TRP B 1 139 ? -0.027  43.281  24.523  1.00 33.92 ? 140 TRP B CG  1 
ATOM   3981 C CD1 . TRP B 1 139 ? 0.750   42.580  23.638  1.00 31.05 ? 140 TRP B CD1 1 
ATOM   3982 C CD2 . TRP B 1 139 ? -0.936  44.057  23.727  1.00 31.66 ? 140 TRP B CD2 1 
ATOM   3983 N NE1 . TRP B 1 139 ? 0.394   42.891  22.343  1.00 29.34 ? 140 TRP B NE1 1 
ATOM   3984 C CE2 . TRP B 1 139 ? -0.638  43.791  22.371  1.00 31.75 ? 140 TRP B CE2 1 
ATOM   3985 C CE3 . TRP B 1 139 ? -1.967  44.951  24.026  1.00 33.97 ? 140 TRP B CE3 1 
ATOM   3986 C CZ2 . TRP B 1 139 ? -1.328  44.401  21.320  1.00 29.91 ? 140 TRP B CZ2 1 
ATOM   3987 C CZ3 . TRP B 1 139 ? -2.649  45.555  22.986  1.00 32.71 ? 140 TRP B CZ3 1 
ATOM   3988 C CH2 . TRP B 1 139 ? -2.333  45.269  21.646  1.00 29.83 ? 140 TRP B CH2 1 
ATOM   3989 N N   . LYS B 1 140 ? 0.925   46.317  25.468  1.00 33.87 ? 141 LYS B N   1 
ATOM   3990 C CA  . LYS B 1 140 ? 0.477   47.610  24.978  1.00 32.87 ? 141 LYS B CA  1 
ATOM   3991 C C   . LYS B 1 140 ? 0.445   47.573  23.458  1.00 30.86 ? 141 LYS B C   1 
ATOM   3992 O O   . LYS B 1 140 ? 1.196   46.812  22.844  1.00 32.99 ? 141 LYS B O   1 
ATOM   3993 C CB  . LYS B 1 140 ? 1.405   48.741  25.455  1.00 35.55 ? 141 LYS B CB  1 
ATOM   3994 C CG  . LYS B 1 140 ? 1.360   48.983  26.948  1.00 37.66 ? 141 LYS B CG  1 
ATOM   3995 C CD  . LYS B 1 140 ? -0.012  49.479  27.370  1.00 45.59 ? 141 LYS B CD  1 
ATOM   3996 C CE  . LYS B 1 140 ? -0.322  50.860  26.779  1.00 46.27 ? 141 LYS B CE  1 
ATOM   3997 N NZ  . LYS B 1 140 ? -1.742  50.966  26.274  1.00 40.50 ? 141 LYS B NZ  1 
ATOM   3998 N N   . PRO B 1 141 ? -0.412  48.375  22.823  1.00 32.40 ? 142 PRO B N   1 
ATOM   3999 C CA  . PRO B 1 141 ? -0.483  48.348  21.358  1.00 31.54 ? 142 PRO B CA  1 
ATOM   4000 C C   . PRO B 1 141 ? 0.727   49.015  20.725  1.00 29.58 ? 142 PRO B C   1 
ATOM   4001 O O   . PRO B 1 141 ? 1.364   49.894  21.319  1.00 30.69 ? 142 PRO B O   1 
ATOM   4002 C CB  . PRO B 1 141 ? -1.767  49.132  21.051  1.00 30.86 ? 142 PRO B CB  1 
ATOM   4003 C CG  . PRO B 1 141 ? -1.888  50.081  22.192  1.00 34.01 ? 142 PRO B CG  1 
ATOM   4004 C CD  . PRO B 1 141 ? -1.381  49.325  23.399  1.00 31.34 ? 142 PRO B CD  1 
ATOM   4005 N N   . LYS B 1 142 ? 1.031   48.585  19.496  1.00 26.30 ? 143 LYS B N   1 
ATOM   4006 C CA  . LYS B 1 142 ? 2.043   49.235  18.665  1.00 26.08 ? 143 LYS B CA  1 
ATOM   4007 C C   . LYS B 1 142 ? 1.402   49.784  17.391  1.00 23.64 ? 143 LYS B C   1 
ATOM   4008 O O   . LYS B 1 142 ? 1.187   50.997  17.267  1.00 25.48 ? 143 LYS B O   1 
ATOM   4009 C CB  . LYS B 1 142 ? 3.179   48.261  18.327  1.00 26.36 ? 143 LYS B CB  1 
ATOM   4010 C CG  . LYS B 1 142 ? 4.348   48.933  17.612  1.00 28.78 ? 143 LYS B CG  1 
ATOM   4011 C CD  . LYS B 1 142 ? 5.555   48.021  17.494  1.00 28.17 ? 143 LYS B CD  1 
ATOM   4012 C CE  . LYS B 1 142 ? 5.319   46.855  16.548  1.00 28.30 ? 143 LYS B CE  1 
ATOM   4013 N NZ  . LYS B 1 142 ? 6.546   46.022  16.504  1.00 28.79 ? 143 LYS B NZ  1 
ATOM   4014 N N   . ASN B 1 143 ? 1.100   48.913  16.432  1.00 23.53 ? 144 ASN B N   1 
ATOM   4015 C CA  . ASN B 1 143 ? 0.380   49.334  15.236  1.00 23.89 ? 144 ASN B CA  1 
ATOM   4016 C C   . ASN B 1 143 ? -1.095  49.544  15.563  1.00 26.63 ? 144 ASN B C   1 
ATOM   4017 O O   . ASN B 1 143 ? -1.608  49.043  16.566  1.00 28.00 ? 144 ASN B O   1 
ATOM   4018 C CB  . ASN B 1 143 ? 0.521   48.293  14.113  1.00 23.42 ? 144 ASN B CB  1 
ATOM   4019 C CG  . ASN B 1 143 ? 1.915   48.279  13.487  1.00 23.78 ? 144 ASN B CG  1 
ATOM   4020 O OD1 . ASN B 1 143 ? 2.418   49.305  13.040  1.00 25.18 ? 144 ASN B OD1 1 
ATOM   4021 N ND2 . ASN B 1 143 ? 2.531   47.101  13.438  1.00 23.26 ? 144 ASN B ND2 1 
ATOM   4022 N N   . SER B 1 144 ? -1.786  50.288  14.696  1.00 23.10 ? 145 SER B N   1 
ATOM   4023 C CA  . SER B 1 144 ? -3.242  50.371  14.796  1.00 25.28 ? 145 SER B CA  1 
ATOM   4024 C C   . SER B 1 144 ? -3.857  48.975  14.752  1.00 26.97 ? 145 SER B C   1 
ATOM   4025 O O   . SER B 1 144 ? -3.522  48.161  13.885  1.00 25.14 ? 145 SER B O   1 
ATOM   4026 C CB  . SER B 1 144 ? -3.794  51.228  13.667  1.00 25.47 ? 145 SER B CB  1 
ATOM   4027 O OG  . SER B 1 144 ? -3.282  52.541  13.792  1.00 32.09 ? 145 SER B OG  1 
ATOM   4028 N N   . ILE B 1 145 ? -4.770  48.698  15.685  1.00 27.31 ? 146 ILE B N   1 
ATOM   4029 C CA  . ILE B 1 145 ? -5.301  47.345  15.811  1.00 25.02 ? 146 ILE B CA  1 
ATOM   4030 C C   . ILE B 1 145 ? -6.084  46.991  14.554  1.00 24.78 ? 146 ILE B C   1 
ATOM   4031 O O   . ILE B 1 145 ? -6.883  47.797  14.051  1.00 24.65 ? 146 ILE B O   1 
ATOM   4032 C CB  . ILE B 1 145 ? -6.160  47.225  17.082  1.00 27.02 ? 146 ILE B CB  1 
ATOM   4033 C CG1 . ILE B 1 145 ? -5.265  47.322  18.325  1.00 24.85 ? 146 ILE B CG1 1 
ATOM   4034 C CG2 . ILE B 1 145 ? -6.936  45.924  17.104  1.00 26.60 ? 146 ILE B CG2 1 
ATOM   4035 C CD1 . ILE B 1 145 ? -6.014  47.615  19.611  1.00 27.22 ? 146 ILE B CD1 1 
ATOM   4036 N N   . GLY B 1 146 ? -5.818  45.796  14.012  1.00 22.93 ? 147 GLY B N   1 
ATOM   4037 C CA  . GLY B 1 146 ? -6.503  45.268  12.848  1.00 25.69 ? 147 GLY B CA  1 
ATOM   4038 C C   . GLY B 1 146 ? -5.846  45.558  11.510  1.00 26.18 ? 147 GLY B C   1 
ATOM   4039 O O   . GLY B 1 146 ? -6.199  44.910  10.511  1.00 26.02 ? 147 GLY B O   1 
ATOM   4040 N N   . GLU B 1 147 ? -4.875  46.470  11.456  1.00 24.34 ? 148 GLU B N   1 
ATOM   4041 C CA  A GLU B 1 147 ? -4.342  46.962  10.184  0.51 24.34 ? 148 GLU B CA  1 
ATOM   4042 C CA  B GLU B 1 147 ? -4.371  46.928  10.169  0.49 24.15 ? 148 GLU B CA  1 
ATOM   4043 C C   . GLU B 1 147 ? -3.107  46.205  9.701   1.00 25.33 ? 148 GLU B C   1 
ATOM   4044 O O   . GLU B 1 147 ? -2.814  46.233  8.499   1.00 22.93 ? 148 GLU B O   1 
ATOM   4045 C CB  A GLU B 1 147 ? -4.001  48.464  10.284  0.51 24.47 ? 148 GLU B CB  1 
ATOM   4046 C CB  B GLU B 1 147 ? -4.141  48.447  10.222  0.49 24.47 ? 148 GLU B CB  1 
ATOM   4047 C CG  A GLU B 1 147 ? -3.767  49.157  8.920   0.51 25.46 ? 148 GLU B CG  1 
ATOM   4048 C CG  B GLU B 1 147 ? -5.387  49.206  10.714  0.49 25.56 ? 148 GLU B CG  1 
ATOM   4049 C CD  A GLU B 1 147 ? -3.211  50.580  9.020   0.51 28.65 ? 148 GLU B CD  1 
ATOM   4050 C CD  B GLU B 1 147 ? -5.384  50.694  10.382  0.49 29.96 ? 148 GLU B CD  1 
ATOM   4051 O OE1 A GLU B 1 147 ? -2.846  51.024  10.132  0.51 27.21 ? 148 GLU B OE1 1 
ATOM   4052 O OE1 B GLU B 1 147 ? -4.327  51.221  9.979   0.49 27.37 ? 148 GLU B OE1 1 
ATOM   4053 O OE2 A GLU B 1 147 ? -3.128  51.261  7.973   0.51 28.18 ? 148 GLU B OE2 1 
ATOM   4054 O OE2 B GLU B 1 147 ? -6.449  51.337  10.524  0.49 30.78 ? 148 GLU B OE2 1 
ATOM   4055 N N   . TYR B 1 148 ? -2.362  45.535  10.593  1.00 20.73 ? 149 TYR B N   1 
ATOM   4056 C CA  . TYR B 1 148 ? -1.117  44.864  10.216  1.00 20.53 ? 149 TYR B CA  1 
ATOM   4057 C C   . TYR B 1 148 ? -1.139  43.391  10.604  1.00 22.92 ? 149 TYR B C   1 
ATOM   4058 O O   . TYR B 1 148 ? -1.406  43.060  11.761  1.00 21.82 ? 149 TYR B O   1 
ATOM   4059 C CB  . TYR B 1 148 ? 0.099   45.552  10.847  1.00 21.33 ? 149 TYR B CB  1 
ATOM   4060 C CG  . TYR B 1 148 ? 0.498   46.754  10.003  1.00 22.67 ? 149 TYR B CG  1 
ATOM   4061 C CD1 . TYR B 1 148 ? -0.232  47.930  10.067  1.00 22.87 ? 149 TYR B CD1 1 
ATOM   4062 C CD2 . TYR B 1 148 ? 1.546   46.669  9.087   1.00 22.13 ? 149 TYR B CD2 1 
ATOM   4063 C CE1 . TYR B 1 148 ? 0.089   49.024  9.251   1.00 22.02 ? 149 TYR B CE1 1 
ATOM   4064 C CE2 . TYR B 1 148 ? 1.873   47.751  8.271   1.00 23.82 ? 149 TYR B CE2 1 
ATOM   4065 C CZ  . TYR B 1 148 ? 1.144   48.914  8.363   1.00 21.89 ? 149 TYR B CZ  1 
ATOM   4066 O OH  . TYR B 1 148 ? 1.463   49.976  7.552   1.00 26.57 ? 149 TYR B OH  1 
ATOM   4067 N N   . ARG B 1 149 ? -0.818  42.523  9.644   1.00 16.58 ? 150 ARG B N   1 
ATOM   4068 C CA  . ARG B 1 149 ? -0.706  41.085  9.886   1.00 18.72 ? 150 ARG B CA  1 
ATOM   4069 C C   . ARG B 1 149 ? 0.730   40.747  10.254  1.00 20.37 ? 150 ARG B C   1 
ATOM   4070 O O   . ARG B 1 149 ? 1.659   41.065  9.505   1.00 20.27 ? 150 ARG B O   1 
ATOM   4071 C CB  . ARG B 1 149 ? -1.124  40.279  8.649   1.00 19.23 ? 150 ARG B CB  1 
ATOM   4072 C CG  . ARG B 1 149 ? -0.954  38.745  8.827   1.00 18.08 ? 150 ARG B CG  1 
ATOM   4073 C CD  . ARG B 1 149 ? -1.057  38.006  7.486   1.00 16.91 ? 150 ARG B CD  1 
ATOM   4074 N NE  . ARG B 1 149 ? -1.130  36.546  7.625   1.00 16.84 ? 150 ARG B NE  1 
ATOM   4075 C CZ  . ARG B 1 149 ? -0.086  35.726  7.642   1.00 21.67 ? 150 ARG B CZ  1 
ATOM   4076 N NH1 . ARG B 1 149 ? 1.155   36.187  7.654   1.00 20.57 ? 150 ARG B NH1 1 
ATOM   4077 N NH2 . ARG B 1 149 ? -0.294  34.400  7.651   1.00 19.67 ? 150 ARG B NH2 1 
ATOM   4078 N N   . GLN B 1 150 ? 0.918   40.103  11.405  1.00 22.13 ? 151 GLN B N   1 
ATOM   4079 C CA  . GLN B 1 150 ? 2.221   39.553  11.768  1.00 21.10 ? 151 GLN B CA  1 
ATOM   4080 C C   . GLN B 1 150 ? 1.979   38.144  12.296  1.00 21.95 ? 151 GLN B C   1 
ATOM   4081 O O   . GLN B 1 150 ? 1.352   37.976  13.344  1.00 23.80 ? 151 GLN B O   1 
ATOM   4082 C CB  . GLN B 1 150 ? 2.950   40.416  12.804  1.00 22.74 ? 151 GLN B CB  1 
ATOM   4083 C CG  . GLN B 1 150 ? 4.339   39.848  13.151  1.00 25.30 ? 151 GLN B CG  1 
ATOM   4084 C CD  . GLN B 1 150 ? 5.405   40.914  13.381  1.00 32.03 ? 151 GLN B CD  1 
ATOM   4085 O OE1 . GLN B 1 150 ? 5.107   42.095  13.569  1.00 33.81 ? 151 GLN B OE1 1 
ATOM   4086 N NE2 . GLN B 1 150 ? 6.663   40.488  13.373  1.00 38.13 ? 151 GLN B NE2 1 
ATOM   4087 N N   . TYR B 1 151 ? 2.426   37.134  11.545  1.00 21.41 ? 152 TYR B N   1 
ATOM   4088 C CA  . TYR B 1 151 ? 2.182   35.740  11.926  1.00 23.17 ? 152 TYR B CA  1 
ATOM   4089 C C   . TYR B 1 151 ? 2.676   35.487  13.344  1.00 21.78 ? 152 TYR B C   1 
ATOM   4090 O O   . TYR B 1 151 ? 3.825   35.790  13.671  1.00 23.65 ? 152 TYR B O   1 
ATOM   4091 C CB  . TYR B 1 151 ? 2.882   34.814  10.930  1.00 23.11 ? 152 TYR B CB  1 
ATOM   4092 C CG  . TYR B 1 151 ? 2.543   33.338  11.052  1.00 24.89 ? 152 TYR B CG  1 
ATOM   4093 C CD1 . TYR B 1 151 ? 1.254   32.880  10.794  1.00 23.89 ? 152 TYR B CD1 1 
ATOM   4094 C CD2 . TYR B 1 151 ? 3.518   32.409  11.386  1.00 29.41 ? 152 TYR B CD2 1 
ATOM   4095 C CE1 . TYR B 1 151 ? 0.935   31.525  10.883  1.00 27.49 ? 152 TYR B CE1 1 
ATOM   4096 C CE2 . TYR B 1 151 ? 3.209   31.042  11.486  1.00 30.98 ? 152 TYR B CE2 1 
ATOM   4097 C CZ  . TYR B 1 151 ? 1.912   30.619  11.224  1.00 30.32 ? 152 TYR B CZ  1 
ATOM   4098 O OH  . TYR B 1 151 ? 1.571   29.286  11.297  1.00 33.66 ? 152 TYR B OH  1 
ATOM   4099 N N   . SER B 1 152 ? 1.796   34.952  14.200  1.00 23.32 ? 153 SER B N   1 
ATOM   4100 C CA  . SER B 1 152 ? 2.078   34.968  15.635  1.00 24.58 ? 153 SER B CA  1 
ATOM   4101 C C   . SER B 1 152 ? 1.459   33.783  16.359  1.00 23.92 ? 153 SER B C   1 
ATOM   4102 O O   . SER B 1 152 ? 0.235   33.599  16.326  1.00 23.82 ? 153 SER B O   1 
ATOM   4103 C CB  . SER B 1 152 ? 1.556   36.251  16.285  1.00 25.00 ? 153 SER B CB  1 
ATOM   4104 O OG  . SER B 1 152 ? 1.727   36.203  17.696  1.00 25.37 ? 153 SER B OG  1 
ATOM   4105 N N   . ASN B 1 153 ? 2.291   33.044  17.081  1.00 25.32 ? 154 ASN B N   1 
ATOM   4106 C CA  . ASN B 1 153 ? 1.801   31.931  17.889  1.00 25.50 ? 154 ASN B CA  1 
ATOM   4107 C C   . ASN B 1 153 ? 1.097   32.410  19.153  1.00 26.68 ? 154 ASN B C   1 
ATOM   4108 O O   . ASN B 1 153 ? 0.038   31.860  19.488  1.00 28.27 ? 154 ASN B O   1 
ATOM   4109 C CB  . ASN B 1 153 ? 2.941   30.967  18.238  1.00 27.78 ? 154 ASN B CB  1 
ATOM   4110 C CG  . ASN B 1 153 ? 3.352   30.117  17.057  1.00 27.84 ? 154 ASN B CG  1 
ATOM   4111 O OD1 . ASN B 1 153 ? 2.506   29.665  16.281  1.00 27.59 ? 154 ASN B OD1 1 
ATOM   4112 N ND2 . ASN B 1 153 ? 4.650   29.913  16.895  1.00 29.39 ? 154 ASN B ND2 1 
ATOM   4113 N N   . PRO B 1 154 ? 1.622   33.407  19.889  1.00 30.81 ? 155 PRO B N   1 
ATOM   4114 C CA  . PRO B 1 154 ? 0.857   33.906  21.047  1.00 28.09 ? 155 PRO B CA  1 
ATOM   4115 C C   . PRO B 1 154 ? -0.509  34.459  20.680  1.00 28.42 ? 155 PRO B C   1 
ATOM   4116 O O   . PRO B 1 154 ? -1.446  34.338  21.479  1.00 28.11 ? 155 PRO B O   1 
ATOM   4117 C CB  . PRO B 1 154 ? 1.764   34.995  21.651  1.00 31.69 ? 155 PRO B CB  1 
ATOM   4118 C CG  . PRO B 1 154 ? 2.863   35.218  20.685  1.00 32.07 ? 155 PRO B CG  1 
ATOM   4119 C CD  . PRO B 1 154 ? 2.985   33.975  19.859  1.00 27.63 ? 155 PRO B CD  1 
ATOM   4120 N N   . SER B 1 155 ? -0.650  35.057  19.496  1.00 26.11 ? 156 SER B N   1 
ATOM   4121 C CA  . SER B 1 155 ? -1.935  35.609  19.074  1.00 28.81 ? 156 SER B CA  1 
ATOM   4122 C C   . SER B 1 155 ? -2.998  34.520  18.946  1.00 25.75 ? 156 SER B C   1 
ATOM   4123 O O   . SER B 1 155 ? -4.067  34.602  19.559  1.00 25.99 ? 156 SER B O   1 
ATOM   4124 C CB  . SER B 1 155 ? -1.763  36.363  17.750  1.00 26.36 ? 156 SER B CB  1 
ATOM   4125 O OG  . SER B 1 155 ? -2.937  37.067  17.408  1.00 27.37 ? 156 SER B OG  1 
ATOM   4126 N N   . ILE B 1 156 ? -2.742  33.498  18.129  1.00 25.23 ? 157 ILE B N   1 
ATOM   4127 C CA  . ILE B 1 156 ? -3.753  32.456  18.013  1.00 25.83 ? 157 ILE B CA  1 
ATOM   4128 C C   . ILE B 1 156 ? -3.766  31.572  19.261  1.00 27.03 ? 157 ILE B C   1 
ATOM   4129 O O   . ILE B 1 156 ? -4.790  30.948  19.562  1.00 29.31 ? 157 ILE B O   1 
ATOM   4130 C CB  . ILE B 1 156 ? -3.566  31.653  16.704  1.00 28.69 ? 157 ILE B CB  1 
ATOM   4131 C CG1 . ILE B 1 156 ? -4.847  30.869  16.361  1.00 28.85 ? 157 ILE B CG1 1 
ATOM   4132 C CG2 . ILE B 1 156 ? -2.366  30.745  16.799  1.00 30.52 ? 157 ILE B CG2 1 
ATOM   4133 C CD1 . ILE B 1 156 ? -4.797  30.159  15.002  1.00 28.19 ? 157 ILE B CD1 1 
ATOM   4134 N N   . GLY B 1 157 ? -2.673  31.543  20.032  1.00 26.74 ? 158 GLY B N   1 
ATOM   4135 C CA  . GLY B 1 157 ? -2.710  30.856  21.317  1.00 30.04 ? 158 GLY B CA  1 
ATOM   4136 C C   . GLY B 1 157 ? -3.708  31.468  22.284  1.00 29.64 ? 158 GLY B C   1 
ATOM   4137 O O   . GLY B 1 157 ? -4.434  30.752  22.977  1.00 29.45 ? 158 GLY B O   1 
ATOM   4138 N N   . LEU B 1 158 ? -3.762  32.808  22.346  1.00 30.33 ? 159 LEU B N   1 
ATOM   4139 C CA  . LEU B 1 158 ? -4.757  33.460  23.193  1.00 27.66 ? 159 LEU B CA  1 
ATOM   4140 C C   . LEU B 1 158 ? -6.168  33.215  22.661  1.00 30.96 ? 159 LEU B C   1 
ATOM   4141 O O   . LEU B 1 158 ? -7.116  33.055  23.441  1.00 34.47 ? 159 LEU B O   1 
ATOM   4142 C CB  . LEU B 1 158 ? -4.460  34.967  23.292  1.00 27.72 ? 159 LEU B CB  1 
ATOM   4143 C CG  . LEU B 1 158 ? -5.366  35.836  24.176  1.00 29.61 ? 159 LEU B CG  1 
ATOM   4144 C CD1 . LEU B 1 158 ? -5.402  35.316  25.598  1.00 33.51 ? 159 LEU B CD1 1 
ATOM   4145 C CD2 . LEU B 1 158 ? -4.915  37.297  24.164  1.00 31.11 ? 159 LEU B CD2 1 
ATOM   4146 N N   . PHE B 1 159 ? -6.322  33.175  21.335  1.00 27.48 ? 160 PHE B N   1 
ATOM   4147 C CA  . PHE B 1 159 ? -7.614  32.848  20.733  1.00 28.00 ? 160 PHE B CA  1 
ATOM   4148 C C   . PHE B 1 159 ? -8.073  31.452  21.139  1.00 31.53 ? 160 PHE B C   1 
ATOM   4149 O O   . PHE B 1 159 ? -9.231  31.252  21.522  1.00 29.31 ? 160 PHE B O   1 
ATOM   4150 C CB  . PHE B 1 159 ? -7.520  32.961  19.209  1.00 28.05 ? 160 PHE B CB  1 
ATOM   4151 C CG  . PHE B 1 159 ? -8.776  32.538  18.476  1.00 30.67 ? 160 PHE B CG  1 
ATOM   4152 C CD1 . PHE B 1 159 ? -9.895  33.358  18.451  1.00 31.61 ? 160 PHE B CD1 1 
ATOM   4153 C CD2 . PHE B 1 159 ? -8.818  31.334  17.787  1.00 29.92 ? 160 PHE B CD2 1 
ATOM   4154 C CE1 . PHE B 1 159 ? -11.044 32.973  17.770  1.00 29.30 ? 160 PHE B CE1 1 
ATOM   4155 C CE2 . PHE B 1 159 ? -9.960  30.940  17.092  1.00 27.70 ? 160 PHE B CE2 1 
ATOM   4156 C CZ  . PHE B 1 159 ? -11.070 31.752  17.085  1.00 30.17 ? 160 PHE B CZ  1 
ATOM   4157 N N   . GLY B 1 160 ? -7.171  30.470  21.065  1.00 30.99 ? 161 GLY B N   1 
ATOM   4158 C CA  . GLY B 1 160 ? -7.534  29.114  21.462  1.00 31.20 ? 161 GLY B CA  1 
ATOM   4159 C C   . GLY B 1 160 ? -7.874  28.989  22.939  1.00 35.38 ? 161 GLY B C   1 
ATOM   4160 O O   . GLY B 1 160 ? -8.810  28.275  23.314  1.00 35.69 ? 161 GLY B O   1 
ATOM   4161 N N   . LYS B 1 161 ? -7.113  29.672  23.800  1.00 35.09 ? 162 LYS B N   1 
ATOM   4162 C CA  . LYS B 1 161 ? -7.416  29.651  25.230  1.00 37.10 ? 162 LYS B CA  1 
ATOM   4163 C C   . LYS B 1 161 ? -8.797  30.230  25.513  1.00 37.85 ? 162 LYS B C   1 
ATOM   4164 O O   . LYS B 1 161 ? -9.523  29.723  26.373  1.00 39.80 ? 162 LYS B O   1 
ATOM   4165 C CB  . LYS B 1 161 ? -6.355  30.423  26.014  1.00 38.33 ? 162 LYS B CB  1 
ATOM   4166 C CG  . LYS B 1 161 ? -6.685  30.548  27.508  1.00 44.33 ? 162 LYS B CG  1 
ATOM   4167 C CD  . LYS B 1 161 ? -5.487  30.988  28.324  1.00 47.19 ? 162 LYS B CD  1 
ATOM   4168 C CE  . LYS B 1 161 ? -5.778  30.942  29.822  1.00 49.15 ? 162 LYS B CE  1 
ATOM   4169 N NZ  . LYS B 1 161 ? -6.201  29.596  30.270  1.00 46.87 ? 162 LYS B NZ  1 
ATOM   4170 N N   . VAL B 1 162 ? -9.165  31.302  24.806  1.00 36.81 ? 163 VAL B N   1 
ATOM   4171 C CA  . VAL B 1 162 ? -10.470 31.937  24.984  1.00 35.74 ? 163 VAL B CA  1 
ATOM   4172 C C   . VAL B 1 162 ? -11.581 31.039  24.456  1.00 38.31 ? 163 VAL B C   1 
ATOM   4173 O O   . VAL B 1 162 ? -12.647 30.922  25.072  1.00 38.94 ? 163 VAL B O   1 
ATOM   4174 C CB  . VAL B 1 162 ? -10.486 33.316  24.295  1.00 39.32 ? 163 VAL B CB  1 
ATOM   4175 C CG1 . VAL B 1 162 ? -11.910 33.841  24.172  1.00 39.38 ? 163 VAL B CG1 1 
ATOM   4176 C CG2 . VAL B 1 162 ? -9.622  34.312  25.066  1.00 39.37 ? 163 VAL B CG2 1 
ATOM   4177 N N   . VAL B 1 163 ? -11.361 30.405  23.302  1.00 32.69 ? 164 VAL B N   1 
ATOM   4178 C CA  . VAL B 1 163 ? -12.343 29.453  22.785  1.00 40.60 ? 164 VAL B CA  1 
ATOM   4179 C C   . VAL B 1 163 ? -12.609 28.361  23.815  1.00 39.82 ? 164 VAL B C   1 
ATOM   4180 O O   . VAL B 1 163 ? -13.762 28.018  24.099  1.00 42.00 ? 164 VAL B O   1 
ATOM   4181 C CB  . VAL B 1 163 ? -11.869 28.856  21.447  1.00 34.39 ? 164 VAL B CB  1 
ATOM   4182 C CG1 . VAL B 1 163 ? -12.721 27.661  21.079  1.00 38.08 ? 164 VAL B CG1 1 
ATOM   4183 C CG2 . VAL B 1 163 ? -11.919 29.917  20.344  1.00 34.83 ? 164 VAL B CG2 1 
ATOM   4184 N N   . ALA B 1 164 ? -11.542 27.818  24.406  1.00 38.12 ? 165 ALA B N   1 
ATOM   4185 C CA  . ALA B 1 164 ? -11.701 26.782  25.419  1.00 39.97 ? 165 ALA B CA  1 
ATOM   4186 C C   . ALA B 1 164 ? -12.411 27.311  26.663  1.00 44.63 ? 165 ALA B C   1 
ATOM   4187 O O   . ALA B 1 164 ? -13.182 26.580  27.294  1.00 46.82 ? 165 ALA B O   1 
ATOM   4188 C CB  . ALA B 1 164 ? -10.335 26.203  25.780  1.00 40.43 ? 165 ALA B CB  1 
ATOM   4189 N N   . LEU B 1 165 ? -12.175 28.572  27.034  1.00 40.73 ? 166 LEU B N   1 
ATOM   4190 C CA  . LEU B 1 165 ? -12.906 29.126  28.170  1.00 44.17 ? 166 LEU B CA  1 
ATOM   4191 C C   . LEU B 1 165 ? -14.397 29.193  27.875  1.00 44.94 ? 166 LEU B C   1 
ATOM   4192 O O   . LEU B 1 165 ? -15.225 28.858  28.729  1.00 49.29 ? 166 LEU B O   1 
ATOM   4193 C CB  . LEU B 1 165 ? -12.377 30.516  28.529  1.00 44.60 ? 166 LEU B CB  1 
ATOM   4194 C CG  . LEU B 1 165 ? -11.003 30.607  29.195  1.00 44.59 ? 166 LEU B CG  1 
ATOM   4195 C CD1 . LEU B 1 165 ? -10.643 32.058  29.475  1.00 45.42 ? 166 LEU B CD1 1 
ATOM   4196 C CD2 . LEU B 1 165 ? -10.965 29.787  30.469  1.00 47.85 ? 166 LEU B CD2 1 
ATOM   4197 N N   . SER B 1 166 ? -14.758 29.618  26.666  1.00 45.13 ? 167 SER B N   1 
ATOM   4198 C CA  . SER B 1 166 ? -16.167 29.744  26.321  1.00 46.57 ? 167 SER B CA  1 
ATOM   4199 C C   . SER B 1 166 ? -16.883 28.408  26.338  1.00 49.20 ? 167 SER B C   1 
ATOM   4200 O O   . SER B 1 166 ? -18.115 28.389  26.404  1.00 48.43 ? 167 SER B O   1 
ATOM   4201 C CB  . SER B 1 166 ? -16.323 30.370  24.940  1.00 46.30 ? 167 SER B CB  1 
ATOM   4202 O OG  . SER B 1 166 ? -16.031 29.427  23.921  1.00 44.15 ? 167 SER B OG  1 
ATOM   4203 N N   . MET B 1 167 ? -16.142 27.299  26.254  1.00 45.29 ? 168 MET B N   1 
ATOM   4204 C CA  . MET B 1 167 ? -16.704 25.957  26.268  1.00 51.47 ? 168 MET B CA  1 
ATOM   4205 C C   . MET B 1 167 ? -16.534 25.249  27.606  1.00 55.44 ? 168 MET B C   1 
ATOM   4206 O O   . MET B 1 167 ? -16.972 24.102  27.740  1.00 54.97 ? 168 MET B O   1 
ATOM   4207 C CB  . MET B 1 167 ? -16.069 25.113  25.159  1.00 48.86 ? 168 MET B CB  1 
ATOM   4208 C CG  . MET B 1 167 ? -16.598 25.430  23.781  1.00 46.04 ? 168 MET B CG  1 
ATOM   4209 S SD  . MET B 1 167 ? -15.435 24.970  22.498  1.00 53.32 ? 168 MET B SD  1 
ATOM   4210 C CE  . MET B 1 167 ? -16.563 24.772  21.132  1.00 50.81 ? 168 MET B CE  1 
ATOM   4211 N N   . ASN B 1 168 ? -15.899 25.895  28.585  1.00 52.68 ? 169 ASN B N   1 
ATOM   4212 C CA  . ASN B 1 168 ? -15.723 25.335  29.928  1.00 55.63 ? 169 ASN B CA  1 
ATOM   4213 C C   . ASN B 1 168 ? -15.014 23.980  29.888  1.00 56.15 ? 169 ASN B C   1 
ATOM   4214 O O   . ASN B 1 168 ? -15.406 23.033  30.570  1.00 54.74 ? 169 ASN B O   1 
ATOM   4215 C CB  . ASN B 1 168 ? -17.068 25.233  30.654  1.00 62.21 ? 169 ASN B CB  1 
ATOM   4216 C CG  . ASN B 1 168 ? -17.928 26.475  30.458  1.00 69.43 ? 169 ASN B CG  1 
ATOM   4217 O OD1 . ASN B 1 168 ? -18.810 26.504  29.597  1.00 73.09 ? 169 ASN B OD1 1 
ATOM   4218 N ND2 . ASN B 1 168 ? -17.662 27.514  31.246  1.00 66.89 ? 169 ASN B ND2 1 
ATOM   4219 N N   . LYS B 1 169 ? -13.965 23.887  29.075  1.00 50.37 ? 170 LYS B N   1 
ATOM   4220 C CA  . LYS B 1 169 ? -13.139 22.695  28.965  1.00 49.24 ? 170 LYS B CA  1 
ATOM   4221 C C   . LYS B 1 169 ? -11.711 23.132  28.687  1.00 47.25 ? 170 LYS B C   1 
ATOM   4222 O O   . LYS B 1 169 ? -11.501 24.156  28.024  1.00 48.63 ? 170 LYS B O   1 
ATOM   4223 C CB  . LYS B 1 169 ? -13.620 21.765  27.840  1.00 50.14 ? 170 LYS B CB  1 
ATOM   4224 C CG  . LYS B 1 169 ? -15.066 21.297  27.961  1.00 57.79 ? 170 LYS B CG  1 
ATOM   4225 C CD  . LYS B 1 169 ? -15.609 20.870  26.604  1.00 59.04 ? 170 LYS B CD  1 
ATOM   4226 C CE  . LYS B 1 169 ? -17.121 21.050  26.529  1.00 57.68 ? 170 LYS B CE  1 
ATOM   4227 N NZ  . LYS B 1 169 ? -17.531 21.506  25.164  1.00 55.31 ? 170 LYS B NZ  1 
ATOM   4228 N N   . PRO B 1 170 ? -10.715 22.390  29.170  1.00 48.37 ? 171 PRO B N   1 
ATOM   4229 C CA  . PRO B 1 170 ? -9.334  22.642  28.736  1.00 43.14 ? 171 PRO B CA  1 
ATOM   4230 C C   . PRO B 1 170 ? -9.219  22.492  27.224  1.00 45.81 ? 171 PRO B C   1 
ATOM   4231 O O   . PRO B 1 170 ? -9.968  21.736  26.599  1.00 42.19 ? 171 PRO B O   1 
ATOM   4232 C CB  . PRO B 1 170 ? -8.521  21.564  29.468  1.00 46.64 ? 171 PRO B CB  1 
ATOM   4233 C CG  . PRO B 1 170 ? -9.418  21.068  30.584  1.00 44.28 ? 171 PRO B CG  1 
ATOM   4234 C CD  . PRO B 1 170 ? -10.822 21.239  30.087  1.00 46.34 ? 171 PRO B CD  1 
ATOM   4235 N N   . PHE B 1 171 ? -8.275  23.228  26.629  1.00 39.54 ? 172 PHE B N   1 
ATOM   4236 C CA  . PHE B 1 171 ? -8.190  23.224  25.172  1.00 41.97 ? 172 PHE B CA  1 
ATOM   4237 C C   . PHE B 1 171 ? -7.976  21.814  24.631  1.00 37.73 ? 172 PHE B C   1 
ATOM   4238 O O   . PHE B 1 171 ? -8.622  21.421  23.653  1.00 38.90 ? 172 PHE B O   1 
ATOM   4239 C CB  . PHE B 1 171 ? -7.081  24.150  24.679  1.00 38.22 ? 172 PHE B CB  1 
ATOM   4240 C CG  . PHE B 1 171 ? -6.960  24.183  23.178  1.00 38.18 ? 172 PHE B CG  1 
ATOM   4241 C CD1 . PHE B 1 171 ? -7.739  25.045  22.428  1.00 35.69 ? 172 PHE B CD1 1 
ATOM   4242 C CD2 . PHE B 1 171 ? -6.087  23.323  22.514  1.00 35.57 ? 172 PHE B CD2 1 
ATOM   4243 C CE1 . PHE B 1 171 ? -7.638  25.071  21.035  1.00 35.96 ? 172 PHE B CE1 1 
ATOM   4244 C CE2 . PHE B 1 171 ? -5.981  23.343  21.138  1.00 32.08 ? 172 PHE B CE2 1 
ATOM   4245 C CZ  . PHE B 1 171 ? -6.756  24.218  20.394  1.00 30.91 ? 172 PHE B CZ  1 
ATOM   4246 N N   . ASP B 1 172 ? -7.072  21.041  25.245  1.00 34.08 ? 173 ASP B N   1 
ATOM   4247 C CA  . ASP B 1 172 ? -6.807  19.693  24.744  1.00 40.21 ? 173 ASP B CA  1 
ATOM   4248 C C   . ASP B 1 172 ? -8.071  18.842  24.759  1.00 39.50 ? 173 ASP B C   1 
ATOM   4249 O O   . ASP B 1 172 ? -8.235  17.948  23.918  1.00 39.52 ? 173 ASP B O   1 
ATOM   4250 C CB  . ASP B 1 172 ? -5.691  19.021  25.554  1.00 38.46 ? 173 ASP B CB  1 
ATOM   4251 C CG  . ASP B 1 172 ? -6.091  18.741  26.991  1.00 48.35 ? 173 ASP B CG  1 
ATOM   4252 O OD1 . ASP B 1 172 ? -6.582  19.671  27.663  1.00 48.14 ? 173 ASP B OD1 1 
ATOM   4253 O OD2 . ASP B 1 172 ? -5.922  17.587  27.455  1.00 51.60 ? 173 ASP B OD2 1 
ATOM   4254 N N   . GLN B 1 173 ? -8.986  19.135  25.685  1.00 41.06 ? 174 GLN B N   1 
ATOM   4255 C CA  . GLN B 1 173 ? -10.258 18.425  25.756  1.00 41.11 ? 174 GLN B CA  1 
ATOM   4256 C C   . GLN B 1 173 ? -11.214 18.861  24.653  1.00 39.76 ? 174 GLN B C   1 
ATOM   4257 O O   . GLN B 1 173 ? -11.945 18.029  24.100  1.00 38.78 ? 174 GLN B O   1 
ATOM   4258 C CB  . GLN B 1 173 ? -10.888 18.652  27.125  1.00 46.68 ? 174 GLN B CB  1 
ATOM   4259 C CG  . GLN B 1 173 ? -10.178 17.899  28.203  1.00 47.56 ? 174 GLN B CG  1 
ATOM   4260 C CD  . GLN B 1 173 ? -10.384 16.424  28.057  1.00 55.17 ? 174 GLN B CD  1 
ATOM   4261 O OE1 . GLN B 1 173 ? -9.451  15.659  27.819  1.00 57.49 ? 174 GLN B OE1 1 
ATOM   4262 N NE2 . GLN B 1 173 ? -11.627 16.008  28.206  1.00 62.16 ? 174 GLN B NE2 1 
ATOM   4263 N N   . VAL B 1 174 ? -11.236 20.164  24.338  1.00 41.38 ? 175 VAL B N   1 
ATOM   4264 C CA  . VAL B 1 174 ? -12.073 20.669  23.249  1.00 35.03 ? 175 VAL B CA  1 
ATOM   4265 C C   . VAL B 1 174 ? -11.806 19.896  21.965  1.00 36.74 ? 175 VAL B C   1 
ATOM   4266 O O   . VAL B 1 174 ? -12.735 19.510  21.247  1.00 37.25 ? 175 VAL B O   1 
ATOM   4267 C CB  . VAL B 1 174 ? -11.838 22.181  23.049  1.00 39.84 ? 175 VAL B CB  1 
ATOM   4268 C CG1 . VAL B 1 174 ? -12.465 22.644  21.752  1.00 35.58 ? 175 VAL B CG1 1 
ATOM   4269 C CG2 . VAL B 1 174 ? -12.406 22.977  24.220  1.00 42.03 ? 175 VAL B CG2 1 
ATOM   4270 N N   . LEU B 1 175 ? -10.533 19.655  21.653  1.00 35.32 ? 176 LEU B N   1 
ATOM   4271 C CA  . LEU B 1 175 ? -10.211 18.939  20.425  1.00 31.71 ? 176 LEU B CA  1 
ATOM   4272 C C   . LEU B 1 175 ? -10.504 17.448  20.560  1.00 35.24 ? 176 LEU B C   1 
ATOM   4273 O O   . LEU B 1 175 ? -11.211 16.871  19.729  1.00 34.55 ? 176 LEU B O   1 
ATOM   4274 C CB  . LEU B 1 175 ? -8.744  19.168  20.047  1.00 28.00 ? 176 LEU B CB  1 
ATOM   4275 C CG  . LEU B 1 175 ? -8.357  20.587  19.607  1.00 29.77 ? 176 LEU B CG  1 
ATOM   4276 C CD1 . LEU B 1 175 ? -6.940  20.611  19.051  1.00 29.39 ? 176 LEU B CD1 1 
ATOM   4277 C CD2 . LEU B 1 175 ? -9.332  21.096  18.565  1.00 30.23 ? 176 LEU B CD2 1 
ATOM   4278 N N   . GLU B 1 176 ? -9.974  16.813  21.607  1.00 34.15 ? 177 GLU B N   1 
ATOM   4279 C CA  . GLU B 1 176 ? -10.001 15.353  21.673  1.00 32.98 ? 177 GLU B CA  1 
ATOM   4280 C C   . GLU B 1 176 ? -11.396 14.818  21.959  1.00 38.84 ? 177 GLU B C   1 
ATOM   4281 O O   . GLU B 1 176 ? -11.743 13.724  21.497  1.00 39.28 ? 177 GLU B O   1 
ATOM   4282 C CB  . GLU B 1 176 ? -8.997  14.861  22.717  1.00 36.50 ? 177 GLU B CB  1 
ATOM   4283 C CG  . GLU B 1 176 ? -7.550  14.913  22.199  1.00 36.22 ? 177 GLU B CG  1 
ATOM   4284 C CD  . GLU B 1 176 ? -6.510  14.534  23.240  1.00 38.43 ? 177 GLU B CD  1 
ATOM   4285 O OE1 . GLU B 1 176 ? -6.901  14.131  24.353  1.00 40.75 ? 177 GLU B OE1 1 
ATOM   4286 O OE2 . GLU B 1 176 ? -5.295  14.641  22.945  1.00 35.84 ? 177 GLU B OE2 1 
ATOM   4287 N N   . LYS B 1 177 ? -12.221 15.569  22.685  1.00 38.58 ? 178 LYS B N   1 
ATOM   4288 C CA  . LYS B 1 177 ? -13.540 15.079  23.049  1.00 43.51 ? 178 LYS B CA  1 
ATOM   4289 C C   . LYS B 1 177 ? -14.679 15.705  22.258  1.00 39.73 ? 178 LYS B C   1 
ATOM   4290 O O   . LYS B 1 177 ? -15.796 15.187  22.317  1.00 41.98 ? 178 LYS B O   1 
ATOM   4291 C CB  . LYS B 1 177 ? -13.793 15.280  24.555  1.00 44.49 ? 178 LYS B CB  1 
ATOM   4292 C CG  . LYS B 1 177 ? -13.094 14.230  25.427  1.00 52.88 ? 178 LYS B CG  1 
ATOM   4293 C CD  . LYS B 1 177 ? -13.825 13.995  26.753  1.00 59.84 ? 178 LYS B CD  1 
ATOM   4294 C CE  . LYS B 1 177 ? -13.399 12.689  27.410  1.00 65.66 ? 178 LYS B CE  1 
ATOM   4295 N NZ  . LYS B 1 177 ? -12.008 12.738  27.920  1.00 69.03 ? 178 LYS B NZ  1 
ATOM   4296 N N   . THR B 1 178 ? -14.440 16.788  21.521  1.00 41.29 ? 179 THR B N   1 
ATOM   4297 C CA  . THR B 1 178 ? -15.514 17.460  20.794  1.00 38.47 ? 179 THR B CA  1 
ATOM   4298 C C   . THR B 1 178 ? -15.210 17.597  19.308  1.00 37.43 ? 179 THR B C   1 
ATOM   4299 O O   . THR B 1 178 ? -16.016 17.155  18.483  1.00 40.01 ? 179 THR B O   1 
ATOM   4300 C CB  . THR B 1 178 ? -15.795 18.843  21.403  1.00 41.75 ? 179 THR B CB  1 
ATOM   4301 O OG1 . THR B 1 178 ? -16.141 18.712  22.788  1.00 42.95 ? 179 THR B OG1 1 
ATOM   4302 C CG2 . THR B 1 178 ? -16.936 19.540  20.654  1.00 40.96 ? 179 THR B CG2 1 
ATOM   4303 N N   . ILE B 1 179 ? -14.076 18.197  18.934  1.00 36.10 ? 180 ILE B N   1 
ATOM   4304 C CA  . ILE B 1 179 ? -13.825 18.511  17.530  1.00 36.64 ? 180 ILE B CA  1 
ATOM   4305 C C   . ILE B 1 179 ? -13.383 17.270  16.755  1.00 35.37 ? 180 ILE B C   1 
ATOM   4306 O O   . ILE B 1 179 ? -13.952 16.949  15.705  1.00 32.11 ? 180 ILE B O   1 
ATOM   4307 C CB  . ILE B 1 179 ? -12.792 19.647  17.404  1.00 37.15 ? 180 ILE B CB  1 
ATOM   4308 C CG1 . ILE B 1 179 ? -13.304 20.925  18.071  1.00 33.41 ? 180 ILE B CG1 1 
ATOM   4309 C CG2 . ILE B 1 179 ? -12.473 19.917  15.941  1.00 32.87 ? 180 ILE B CG2 1 
ATOM   4310 C CD1 . ILE B 1 179 ? -14.710 21.334  17.634  1.00 35.38 ? 180 ILE B CD1 1 
ATOM   4311 N N   . PHE B 1 180 ? -12.341 16.581  17.232  1.00 32.72 ? 181 PHE B N   1 
ATOM   4312 C CA  . PHE B 1 180 ? -11.869 15.386  16.536  1.00 35.78 ? 181 PHE B CA  1 
ATOM   4313 C C   . PHE B 1 180 ? -12.978 14.357  16.342  1.00 36.96 ? 181 PHE B C   1 
ATOM   4314 O O   . PHE B 1 180 ? -13.096 13.818  15.227  1.00 36.89 ? 181 PHE B O   1 
ATOM   4315 C CB  . PHE B 1 180 ? -10.680 14.773  17.282  1.00 33.45 ? 181 PHE B CB  1 
ATOM   4316 C CG  . PHE B 1 180 ? -9.440  15.620  17.286  1.00 29.58 ? 181 PHE B CG  1 
ATOM   4317 C CD1 . PHE B 1 180 ? -9.263  16.658  16.372  1.00 30.46 ? 181 PHE B CD1 1 
ATOM   4318 C CD2 . PHE B 1 180 ? -8.437  15.362  18.205  1.00 29.54 ? 181 PHE B CD2 1 
ATOM   4319 C CE1 . PHE B 1 180 ? -8.104  17.421  16.382  1.00 30.18 ? 181 PHE B CE1 1 
ATOM   4320 C CE2 . PHE B 1 180 ? -7.274  16.104  18.217  1.00 28.62 ? 181 PHE B CE2 1 
ATOM   4321 C CZ  . PHE B 1 180 ? -7.108  17.149  17.306  1.00 29.73 ? 181 PHE B CZ  1 
ATOM   4322 N N   . PRO B 1 181 ? -13.807 14.031  17.349  1.00 35.08 ? 182 PRO B N   1 
ATOM   4323 C CA  . PRO B 1 181 ? -14.919 13.098  17.092  1.00 36.94 ? 182 PRO B CA  1 
ATOM   4324 C C   . PRO B 1 181 ? -15.948 13.632  16.115  1.00 38.86 ? 182 PRO B C   1 
ATOM   4325 O O   . PRO B 1 181 ? -16.489 12.866  15.308  1.00 36.22 ? 182 PRO B O   1 
ATOM   4326 C CB  . PRO B 1 181 ? -15.526 12.889  18.485  1.00 40.63 ? 182 PRO B CB  1 
ATOM   4327 C CG  . PRO B 1 181 ? -14.442 13.235  19.427  1.00 39.12 ? 182 PRO B CG  1 
ATOM   4328 C CD  . PRO B 1 181 ? -13.707 14.358  18.781  1.00 37.06 ? 182 PRO B CD  1 
ATOM   4329 N N   . ALA B 1 182 ? -16.243 14.931  16.164  1.00 40.55 ? 183 ALA B N   1 
ATOM   4330 C CA  . ALA B 1 182 ? -17.158 15.511  15.188  1.00 37.29 ? 183 ALA B CA  1 
ATOM   4331 C C   . ALA B 1 182 ? -16.649 15.332  13.760  1.00 35.40 ? 183 ALA B C   1 
ATOM   4332 O O   . ALA B 1 182 ? -17.450 15.171  12.834  1.00 36.43 ? 183 ALA B O   1 
ATOM   4333 C CB  . ALA B 1 182 ? -17.375 16.992  15.501  1.00 33.87 ? 183 ALA B CB  1 
ATOM   4334 N N   . LEU B 1 183 ? -15.333 15.369  13.555  1.00 34.41 ? 184 LEU B N   1 
ATOM   4335 C CA  . LEU B 1 183 ? -14.742 15.162  12.239  1.00 33.22 ? 184 LEU B CA  1 
ATOM   4336 C C   . LEU B 1 183 ? -14.473 13.692  11.926  1.00 35.45 ? 184 LEU B C   1 
ATOM   4337 O O   . LEU B 1 183 ? -13.917 13.392  10.864  1.00 37.13 ? 184 LEU B O   1 
ATOM   4338 C CB  . LEU B 1 183 ? -13.438 15.954  12.121  1.00 28.91 ? 184 LEU B CB  1 
ATOM   4339 C CG  . LEU B 1 183 ? -13.602 17.468  12.270  1.00 32.83 ? 184 LEU B CG  1 
ATOM   4340 C CD1 . LEU B 1 183 ? -12.258 18.118  12.529  1.00 26.23 ? 184 LEU B CD1 1 
ATOM   4341 C CD2 . LEU B 1 183 ? -14.251 18.032  11.016  1.00 33.65 ? 184 LEU B CD2 1 
ATOM   4342 N N   . GLY B 1 184 ? -14.829 12.779  12.822  1.00 33.70 ? 185 GLY B N   1 
ATOM   4343 C CA  . GLY B 1 184 ? -14.616 11.367  12.568  1.00 36.09 ? 185 GLY B CA  1 
ATOM   4344 C C   . GLY B 1 184 ? -13.168 10.933  12.604  1.00 40.08 ? 185 GLY B C   1 
ATOM   4345 O O   . GLY B 1 184 ? -12.828 9.881   12.056  1.00 40.00 ? 185 GLY B O   1 
ATOM   4346 N N   . LEU B 1 185 ? -12.303 11.711  13.244  1.00 34.30 ? 186 LEU B N   1 
ATOM   4347 C CA  . LEU B 1 185 ? -10.884 11.396  13.322  1.00 33.16 ? 186 LEU B CA  1 
ATOM   4348 C C   . LEU B 1 185 ? -10.645 10.506  14.532  1.00 35.89 ? 186 LEU B C   1 
ATOM   4349 O O   . LEU B 1 185 ? -11.050 10.848  15.647  1.00 38.45 ? 186 LEU B O   1 
ATOM   4350 C CB  . LEU B 1 185 ? -10.063 12.679  13.425  1.00 33.02 ? 186 LEU B CB  1 
ATOM   4351 C CG  . LEU B 1 185 ? -10.472 13.719  12.387  1.00 30.92 ? 186 LEU B CG  1 
ATOM   4352 C CD1 . LEU B 1 185 ? -9.652  14.990  12.529  1.00 31.52 ? 186 LEU B CD1 1 
ATOM   4353 C CD2 . LEU B 1 185 ? -10.351 13.130  10.993  1.00 33.10 ? 186 LEU B CD2 1 
ATOM   4354 N N   . LYS B 1 186 ? -9.982  9.371   14.315  1.00 33.53 ? 187 LYS B N   1 
ATOM   4355 C CA  . LYS B 1 186 ? -9.814  8.376   15.363  1.00 35.76 ? 187 LYS B CA  1 
ATOM   4356 C C   . LYS B 1 186 ? -8.401  8.281   15.926  1.00 32.93 ? 187 LYS B C   1 
ATOM   4357 O O   . LYS B 1 186 ? -8.220  7.666   16.981  1.00 30.97 ? 187 LYS B O   1 
ATOM   4358 C CB  . LYS B 1 186 ? -10.251 7.002   14.838  1.00 38.79 ? 187 LYS B CB  1 
ATOM   4359 C CG  . LYS B 1 186 ? -11.762 6.883   14.665  1.00 44.31 ? 187 LYS B CG  1 
ATOM   4360 C CD  . LYS B 1 186 ? -12.119 6.375   13.272  1.00 49.26 ? 187 LYS B CD  1 
ATOM   4361 C CE  . LYS B 1 186 ? -13.633 6.285   13.076  1.00 51.88 ? 187 LYS B CE  1 
ATOM   4362 N NZ  . LYS B 1 186 ? -14.154 7.376   12.190  1.00 57.19 ? 187 LYS B NZ  1 
ATOM   4363 N N   . HIS B 1 187 ? -7.399  8.862   15.267  1.00 31.59 ? 188 HIS B N   1 
ATOM   4364 C CA  . HIS B 1 187 ? -6.024  8.803   15.767  1.00 31.68 ? 188 HIS B CA  1 
ATOM   4365 C C   . HIS B 1 187 ? -5.350  10.163  15.613  1.00 30.14 ? 188 HIS B C   1 
ATOM   4366 O O   . HIS B 1 187 ? -4.227  10.282  15.118  1.00 29.15 ? 188 HIS B O   1 
ATOM   4367 C CB  . HIS B 1 187 ? -5.229  7.700   15.071  1.00 28.74 ? 188 HIS B CB  1 
ATOM   4368 C CG  . HIS B 1 187 ? -5.741  6.326   15.374  1.00 31.98 ? 188 HIS B CG  1 
ATOM   4369 N ND1 . HIS B 1 187 ? -6.708  5.709   14.613  1.00 35.37 ? 188 HIS B ND1 1 
ATOM   4370 C CD2 . HIS B 1 187 ? -5.459  5.474   16.387  1.00 33.72 ? 188 HIS B CD2 1 
ATOM   4371 C CE1 . HIS B 1 187 ? -6.979  4.521   15.125  1.00 36.30 ? 188 HIS B CE1 1 
ATOM   4372 N NE2 . HIS B 1 187 ? -6.235  4.355   16.204  1.00 36.56 ? 188 HIS B NE2 1 
ATOM   4373 N N   . SER B 1 188 ? -6.046  11.203  16.054  1.00 27.59 ? 189 SER B N   1 
ATOM   4374 C CA  . SER B 1 188 ? -5.504  12.551  16.144  1.00 29.56 ? 189 SER B CA  1 
ATOM   4375 C C   . SER B 1 188 ? -5.506  12.970  17.607  1.00 29.57 ? 189 SER B C   1 
ATOM   4376 O O   . SER B 1 188 ? -6.487  12.737  18.319  1.00 31.41 ? 189 SER B O   1 
ATOM   4377 C CB  . SER B 1 188 ? -6.323  13.519  15.301  1.00 29.37 ? 189 SER B CB  1 
ATOM   4378 O OG  . SER B 1 188 ? -6.365  13.098  13.943  1.00 29.48 ? 189 SER B OG  1 
ATOM   4379 N N   . TYR B 1 189 ? -4.408  13.578  18.062  1.00 28.08 ? 190 TYR B N   1 
ATOM   4380 C CA  . TYR B 1 189 ? -4.208  13.801  19.490  1.00 30.32 ? 190 TYR B CA  1 
ATOM   4381 C C   . TYR B 1 189 ? -3.532  15.139  19.757  1.00 29.01 ? 190 TYR B C   1 
ATOM   4382 O O   . TYR B 1 189 ? -2.732  15.630  18.956  1.00 27.88 ? 190 TYR B O   1 
ATOM   4383 C CB  . TYR B 1 189 ? -3.330  12.713  20.138  1.00 30.51 ? 190 TYR B CB  1 
ATOM   4384 C CG  . TYR B 1 189 ? -3.764  11.293  19.845  1.00 30.88 ? 190 TYR B CG  1 
ATOM   4385 C CD1 . TYR B 1 189 ? -4.789  10.694  20.569  1.00 32.67 ? 190 TYR B CD1 1 
ATOM   4386 C CD2 . TYR B 1 189 ? -3.154  10.555  18.836  1.00 31.65 ? 190 TYR B CD2 1 
ATOM   4387 C CE1 . TYR B 1 189 ? -5.190  9.376   20.296  1.00 34.33 ? 190 TYR B CE1 1 
ATOM   4388 C CE2 . TYR B 1 189 ? -3.545  9.253   18.555  1.00 30.74 ? 190 TYR B CE2 1 
ATOM   4389 C CZ  . TYR B 1 189 ? -4.562  8.671   19.285  1.00 33.81 ? 190 TYR B CZ  1 
ATOM   4390 O OH  . TYR B 1 189 ? -4.951  7.380   19.003  1.00 32.34 ? 190 TYR B OH  1 
ATOM   4391 N N   . VAL B 1 190 ? -3.836  15.699  20.924  1.00 29.55 ? 191 VAL B N   1 
ATOM   4392 C CA  . VAL B 1 190 ? -2.953  16.691  21.525  1.00 32.51 ? 191 VAL B CA  1 
ATOM   4393 C C   . VAL B 1 190 ? -1.913  16.019  22.411  1.00 35.11 ? 191 VAL B C   1 
ATOM   4394 O O   . VAL B 1 190 ? -0.727  16.353  22.347  1.00 34.27 ? 191 VAL B O   1 
ATOM   4395 C CB  . VAL B 1 190 ? -3.771  17.740  22.302  1.00 37.37 ? 191 VAL B CB  1 
ATOM   4396 C CG1 . VAL B 1 190 ? -2.841  18.662  23.077  1.00 36.33 ? 191 VAL B CG1 1 
ATOM   4397 C CG2 . VAL B 1 190 ? -4.633  18.552  21.336  1.00 33.76 ? 191 VAL B CG2 1 
ATOM   4398 N N   . ASN B 1 191 ? -2.337  15.057  23.233  1.00 35.76 ? 192 ASN B N   1 
ATOM   4399 C CA  . ASN B 1 191 ? -1.433  14.207  23.999  1.00 36.98 ? 192 ASN B CA  1 
ATOM   4400 C C   . ASN B 1 191 ? -1.585  12.773  23.508  1.00 35.00 ? 192 ASN B C   1 
ATOM   4401 O O   . ASN B 1 191 ? -2.657  12.179  23.647  1.00 35.66 ? 192 ASN B O   1 
ATOM   4402 C CB  . ASN B 1 191 ? -1.724  14.287  25.497  1.00 37.73 ? 192 ASN B CB  1 
ATOM   4403 C CG  . ASN B 1 191 ? -1.742  15.706  26.001  1.00 42.10 ? 192 ASN B CG  1 
ATOM   4404 O OD1 . ASN B 1 191 ? -0.708  16.372  26.060  1.00 41.86 ? 192 ASN B OD1 1 
ATOM   4405 N ND2 . ASN B 1 191 ? -2.926  16.185  26.364  1.00 44.78 ? 192 ASN B ND2 1 
ATOM   4406 N N   . VAL B 1 192 ? -0.521  12.231  22.933  1.00 35.45 ? 193 VAL B N   1 
ATOM   4407 C CA  . VAL B 1 192 ? -0.553  10.852  22.429  1.00 35.02 ? 193 VAL B CA  1 
ATOM   4408 C C   . VAL B 1 192 ? -0.567  9.886   23.611  1.00 41.52 ? 193 VAL B C   1 
ATOM   4409 O O   . VAL B 1 192 ? 0.316   9.970   24.482  1.00 44.72 ? 193 VAL B O   1 
ATOM   4410 C CB  . VAL B 1 192 ? 0.650   10.596  21.519  1.00 34.88 ? 193 VAL B CB  1 
ATOM   4411 C CG1 . VAL B 1 192 ? 0.664   9.143   21.050  1.00 33.53 ? 193 VAL B CG1 1 
ATOM   4412 C CG2 . VAL B 1 192 ? 0.642   11.553  20.332  1.00 31.47 ? 193 VAL B CG2 1 
ATOM   4413 N N   . PRO B 1 193 ? -1.531  8.966   23.694  1.00 39.90 ? 194 PRO B N   1 
ATOM   4414 C CA  . PRO B 1 193 ? -1.561  8.017   24.815  1.00 41.93 ? 194 PRO B CA  1 
ATOM   4415 C C   . PRO B 1 193 ? -0.470  6.959   24.710  1.00 41.51 ? 194 PRO B C   1 
ATOM   4416 O O   . PRO B 1 193 ? 0.098   6.705   23.647  1.00 39.26 ? 194 PRO B O   1 
ATOM   4417 C CB  . PRO B 1 193 ? -2.953  7.379   24.710  1.00 41.81 ? 194 PRO B CB  1 
ATOM   4418 C CG  . PRO B 1 193 ? -3.347  7.560   23.286  1.00 40.60 ? 194 PRO B CG  1 
ATOM   4419 C CD  . PRO B 1 193 ? -2.715  8.843   22.827  1.00 37.04 ? 194 PRO B CD  1 
ATOM   4420 N N   . LYS B 1 194 ? -0.197  6.326   25.855  1.00 44.07 ? 195 LYS B N   1 
ATOM   4421 C CA  . LYS B 1 194 ? 0.888   5.348   25.934  1.00 43.76 ? 195 LYS B CA  1 
ATOM   4422 C C   . LYS B 1 194 ? 0.698   4.207   24.939  1.00 44.14 ? 195 LYS B C   1 
ATOM   4423 O O   . LYS B 1 194 ? 1.669   3.735   24.337  1.00 44.61 ? 195 LYS B O   1 
ATOM   4424 C CB  . LYS B 1 194 ? 1.002   4.803   27.362  1.00 40.77 ? 195 LYS B CB  1 
ATOM   4425 C CG  . LYS B 1 194 ? 1.975   3.641   27.485  1.00 50.83 ? 195 LYS B CG  1 
ATOM   4426 C CD  . LYS B 1 194 ? 1.295   2.377   28.026  1.00 52.34 ? 195 LYS B CD  1 
ATOM   4427 C CE  . LYS B 1 194 ? 1.875   1.116   27.393  1.00 49.72 ? 195 LYS B CE  1 
ATOM   4428 N NZ  . LYS B 1 194 ? 1.254   -0.122  27.946  1.00 58.82 ? 195 LYS B NZ  1 
ATOM   4429 N N   . THR B 1 195 ? -0.543  3.746   24.755  1.00 41.38 ? 196 THR B N   1 
ATOM   4430 C CA  . THR B 1 195 ? -0.802  2.640   23.839  1.00 45.84 ? 196 THR B CA  1 
ATOM   4431 C C   . THR B 1 195 ? -0.548  3.003   22.378  1.00 40.94 ? 196 THR B C   1 
ATOM   4432 O O   . THR B 1 195 ? -0.560  2.106   21.528  1.00 41.46 ? 196 THR B O   1 
ATOM   4433 C CB  . THR B 1 195 ? -2.241  2.137   24.009  1.00 48.33 ? 196 THR B CB  1 
ATOM   4434 O OG1 . THR B 1 195 ? -3.145  3.242   23.924  1.00 51.61 ? 196 THR B OG1 1 
ATOM   4435 C CG2 . THR B 1 195 ? -2.416  1.452   25.358  1.00 46.66 ? 196 THR B CG2 1 
ATOM   4436 N N   . GLN B 1 196 ? -0.308  4.278   22.067  1.00 37.79 ? 197 GLN B N   1 
ATOM   4437 C CA  . GLN B 1 196 ? 0.049   4.705   20.719  1.00 41.23 ? 197 GLN B CA  1 
ATOM   4438 C C   . GLN B 1 196 ? 1.513   5.122   20.604  1.00 39.24 ? 197 GLN B C   1 
ATOM   4439 O O   . GLN B 1 196 ? 1.929   5.592   19.542  1.00 34.80 ? 197 GLN B O   1 
ATOM   4440 C CB  . GLN B 1 196 ? -0.856  5.857   20.269  1.00 33.04 ? 197 GLN B CB  1 
ATOM   4441 C CG  . GLN B 1 196 ? -2.307  5.468   20.058  1.00 36.63 ? 197 GLN B CG  1 
ATOM   4442 C CD  . GLN B 1 196 ? -2.511  4.618   18.811  1.00 35.88 ? 197 GLN B CD  1 
ATOM   4443 O OE1 . GLN B 1 196 ? -1.798  4.765   17.818  1.00 35.62 ? 197 GLN B OE1 1 
ATOM   4444 N NE2 . GLN B 1 196 ? -3.488  3.733   18.858  1.00 32.86 ? 197 GLN B NE2 1 
ATOM   4445 N N   . MET B 1 197 ? 2.301   4.945   21.667  1.00 38.39 ? 198 MET B N   1 
ATOM   4446 C CA  . MET B 1 197 ? 3.685   5.414   21.669  1.00 39.60 ? 198 MET B CA  1 
ATOM   4447 C C   . MET B 1 197 ? 4.499   4.804   20.530  1.00 36.65 ? 198 MET B C   1 
ATOM   4448 O O   . MET B 1 197 ? 5.293   5.499   19.889  1.00 36.90 ? 198 MET B O   1 
ATOM   4449 C CB  . MET B 1 197 ? 4.339   5.095   23.015  1.00 47.58 ? 198 MET B CB  1 
ATOM   4450 C CG  . MET B 1 197 ? 5.334   6.139   23.507  1.00 55.91 ? 198 MET B CG  1 
ATOM   4451 S SD  . MET B 1 197 ? 4.574   7.480   24.460  1.00 75.83 ? 198 MET B SD  1 
ATOM   4452 C CE  . MET B 1 197 ? 4.345   8.776   23.220  1.00 52.02 ? 198 MET B CE  1 
ATOM   4453 N N   . GLN B 1 198 ? 4.317   3.504   20.265  1.00 34.57 ? 199 GLN B N   1 
ATOM   4454 C CA  . GLN B 1 198 ? 5.114   2.822   19.250  1.00 34.80 ? 199 GLN B CA  1 
ATOM   4455 C C   . GLN B 1 198 ? 4.875   3.338   17.830  1.00 34.28 ? 199 GLN B C   1 
ATOM   4456 O O   . GLN B 1 198 ? 5.667   3.005   16.939  1.00 33.04 ? 199 GLN B O   1 
ATOM   4457 C CB  . GLN B 1 198 ? 4.848   1.311   19.287  1.00 36.90 ? 199 GLN B CB  1 
ATOM   4458 C CG  . GLN B 1 198 ? 3.520   0.887   18.656  1.00 38.72 ? 199 GLN B CG  1 
ATOM   4459 C CD  . GLN B 1 198 ? 2.334   1.052   19.599  1.00 45.13 ? 199 GLN B CD  1 
ATOM   4460 O OE1 . GLN B 1 198 ? 2.461   1.624   20.689  1.00 48.03 ? 199 GLN B OE1 1 
ATOM   4461 N NE2 . GLN B 1 198 ? 1.175   0.532   19.191  1.00 48.57 ? 199 GLN B NE2 1 
ATOM   4462 N N   . ASN B 1 199 ? 3.818   4.121   17.594  1.00 33.48 ? 200 ASN B N   1 
ATOM   4463 C CA  . ASN B 1 199 ? 3.479   4.621   16.261  1.00 29.26 ? 200 ASN B CA  1 
ATOM   4464 C C   . ASN B 1 199 ? 3.965   6.041   16.014  1.00 29.01 ? 200 ASN B C   1 
ATOM   4465 O O   . ASN B 1 199 ? 3.802   6.554   14.905  1.00 24.14 ? 200 ASN B O   1 
ATOM   4466 C CB  . ASN B 1 199 ? 1.960   4.563   16.043  1.00 27.52 ? 200 ASN B CB  1 
ATOM   4467 C CG  . ASN B 1 199 ? 1.420   3.148   16.087  1.00 33.41 ? 200 ASN B CG  1 
ATOM   4468 O OD1 . ASN B 1 199 ? 2.086   2.205   15.653  1.00 34.58 ? 200 ASN B OD1 1 
ATOM   4469 N ND2 . ASN B 1 199 ? 0.209   2.989   16.614  1.00 29.63 ? 200 ASN B ND2 1 
ATOM   4470 N N   . TYR B 1 200 ? 4.576   6.671   17.007  1.00 28.73 ? 201 TYR B N   1 
ATOM   4471 C CA  . TYR B 1 200 ? 4.940   8.080   16.922  1.00 28.66 ? 201 TYR B CA  1 
ATOM   4472 C C   . TYR B 1 200 ? 6.268   8.237   16.190  1.00 29.51 ? 201 TYR B C   1 
ATOM   4473 O O   . TYR B 1 200 ? 7.274   7.640   16.584  1.00 35.80 ? 201 TYR B O   1 
ATOM   4474 C CB  . TYR B 1 200 ? 5.037   8.641   18.335  1.00 28.89 ? 201 TYR B CB  1 
ATOM   4475 C CG  . TYR B 1 200 ? 5.192   10.136  18.453  1.00 35.43 ? 201 TYR B CG  1 
ATOM   4476 C CD1 . TYR B 1 200 ? 6.414   10.754  18.227  1.00 38.86 ? 201 TYR B CD1 1 
ATOM   4477 C CD2 . TYR B 1 200 ? 4.123   10.922  18.852  1.00 37.38 ? 201 TYR B CD2 1 
ATOM   4478 C CE1 . TYR B 1 200 ? 6.550   12.136  18.369  1.00 39.77 ? 201 TYR B CE1 1 
ATOM   4479 C CE2 . TYR B 1 200 ? 4.251   12.286  18.999  1.00 38.55 ? 201 TYR B CE2 1 
ATOM   4480 C CZ  . TYR B 1 200 ? 5.459   12.887  18.756  1.00 36.28 ? 201 TYR B CZ  1 
ATOM   4481 O OH  . TYR B 1 200 ? 5.569   14.246  18.924  1.00 36.26 ? 201 TYR B OH  1 
ATOM   4482 N N   . ALA B 1 201 ? 6.275   9.054   15.142  1.00 28.73 ? 202 ALA B N   1 
ATOM   4483 C CA  . ALA B 1 201 ? 7.449   9.222   14.291  1.00 28.19 ? 202 ALA B CA  1 
ATOM   4484 C C   . ALA B 1 201 ? 8.362   10.292  14.885  1.00 33.37 ? 202 ALA B C   1 
ATOM   4485 O O   . ALA B 1 201 ? 8.007   11.477  14.909  1.00 26.89 ? 202 ALA B O   1 
ATOM   4486 C CB  . ALA B 1 201 ? 7.024   9.593   12.872  1.00 26.37 ? 202 ALA B CB  1 
ATOM   4487 N N   . PHE B 1 202 ? 9.550   9.880   15.341  1.00 30.68 ? 203 PHE B N   1 
ATOM   4488 C CA  . PHE B 1 202 ? 10.529  10.828  15.866  1.00 32.79 ? 203 PHE B CA  1 
ATOM   4489 C C   . PHE B 1 202 ? 11.544  11.313  14.834  1.00 36.73 ? 203 PHE B C   1 
ATOM   4490 O O   . PHE B 1 202 ? 12.203  12.331  15.079  1.00 35.62 ? 203 PHE B O   1 
ATOM   4491 C CB  . PHE B 1 202 ? 11.318  10.223  17.028  1.00 32.15 ? 203 PHE B CB  1 
ATOM   4492 C CG  . PHE B 1 202 ? 10.506  9.958   18.260  1.00 40.27 ? 203 PHE B CG  1 
ATOM   4493 C CD1 . PHE B 1 202 ? 10.216  10.978  19.149  1.00 43.75 ? 203 PHE B CD1 1 
ATOM   4494 C CD2 . PHE B 1 202 ? 10.069  8.673   18.555  1.00 38.76 ? 203 PHE B CD2 1 
ATOM   4495 C CE1 . PHE B 1 202 ? 9.490   10.725  20.303  1.00 44.68 ? 203 PHE B CE1 1 
ATOM   4496 C CE2 . PHE B 1 202 ? 9.337   8.415   19.702  1.00 43.13 ? 203 PHE B CE2 1 
ATOM   4497 C CZ  . PHE B 1 202 ? 9.049   9.445   20.577  1.00 45.36 ? 203 PHE B CZ  1 
ATOM   4498 N N   . GLY B 1 203 ? 11.711  10.610  13.712  1.00 31.68 ? 204 GLY B N   1 
ATOM   4499 C CA  . GLY B 1 203 ? 12.688  11.049  12.716  1.00 27.91 ? 204 GLY B CA  1 
ATOM   4500 C C   . GLY B 1 203 ? 14.106  10.936  13.259  1.00 33.99 ? 204 GLY B C   1 
ATOM   4501 O O   . GLY B 1 203 ? 14.484  9.923   13.853  1.00 31.71 ? 204 GLY B O   1 
ATOM   4502 N N   . TYR B 1 204 ? 14.909  11.987  13.055  1.00 32.97 ? 205 TYR B N   1 
ATOM   4503 C CA  . TYR B 1 204 ? 16.246  12.041  13.650  1.00 32.67 ? 205 TYR B CA  1 
ATOM   4504 C C   . TYR B 1 204 ? 16.201  12.333  15.139  1.00 36.27 ? 205 TYR B C   1 
ATOM   4505 O O   . TYR B 1 204 ? 17.192  12.084  15.835  1.00 41.57 ? 205 TYR B O   1 
ATOM   4506 C CB  . TYR B 1 204 ? 17.106  13.118  12.985  1.00 34.63 ? 205 TYR B CB  1 
ATOM   4507 C CG  . TYR B 1 204 ? 17.562  12.805  11.587  1.00 33.23 ? 205 TYR B CG  1 
ATOM   4508 C CD1 . TYR B 1 204 ? 18.608  11.922  11.360  1.00 38.21 ? 205 TYR B CD1 1 
ATOM   4509 C CD2 . TYR B 1 204 ? 16.963  13.412  10.492  1.00 33.74 ? 205 TYR B CD2 1 
ATOM   4510 C CE1 . TYR B 1 204 ? 19.032  11.639  10.070  1.00 40.30 ? 205 TYR B CE1 1 
ATOM   4511 C CE2 . TYR B 1 204 ? 17.376  13.144  9.204   1.00 33.96 ? 205 TYR B CE2 1 
ATOM   4512 C CZ  . TYR B 1 204 ? 18.411  12.255  8.998   1.00 38.81 ? 205 TYR B CZ  1 
ATOM   4513 O OH  . TYR B 1 204 ? 18.822  11.975  7.713   1.00 39.79 ? 205 TYR B OH  1 
ATOM   4514 N N   . ASN B 1 205 ? 15.083  12.868  15.631  1.00 38.37 ? 206 ASN B N   1 
ATOM   4515 C CA  . ASN B 1 205 ? 14.934  13.286  17.022  1.00 41.24 ? 206 ASN B CA  1 
ATOM   4516 C C   . ASN B 1 205 ? 16.143  14.104  17.467  1.00 46.95 ? 206 ASN B C   1 
ATOM   4517 O O   . ASN B 1 205 ? 16.806  13.802  18.464  1.00 44.46 ? 206 ASN B O   1 
ATOM   4518 C CB  . ASN B 1 205 ? 14.709  12.082  17.937  1.00 41.11 ? 206 ASN B CB  1 
ATOM   4519 C CG  . ASN B 1 205 ? 14.156  12.485  19.289  1.00 48.49 ? 206 ASN B CG  1 
ATOM   4520 O OD1 . ASN B 1 205 ? 13.592  13.571  19.435  1.00 47.16 ? 206 ASN B OD1 1 
ATOM   4521 N ND2 . ASN B 1 205 ? 14.310  11.612  20.284  1.00 45.43 ? 206 ASN B ND2 1 
ATOM   4522 N N   . GLN B 1 206 ? 16.436  15.128  16.656  1.00 43.57 ? 207 GLN B N   1 
ATOM   4523 C CA  . GLN B 1 206 ? 17.644  15.966  16.854  1.00 44.65 ? 207 GLN B CA  1 
ATOM   4524 C C   . GLN B 1 206 ? 17.736  16.578  18.252  1.00 49.87 ? 207 GLN B C   1 
ATOM   4525 O O   . GLN B 1 206 ? 18.854  16.916  18.647  1.00 51.85 ? 207 GLN B O   1 
ATOM   4526 C CB  . GLN B 1 206 ? 17.677  17.053  15.779  1.00 43.32 ? 207 GLN B CB  1 
ATOM   4527 C CG  . GLN B 1 206 ? 16.503  18.011  15.770  1.00 43.05 ? 207 GLN B CG  1 
ATOM   4528 C CD  . GLN B 1 206 ? 16.702  18.999  14.647  1.00 43.94 ? 207 GLN B CD  1 
ATOM   4529 O OE1 . GLN B 1 206 ? 17.823  19.412  14.359  1.00 40.76 ? 207 GLN B OE1 1 
ATOM   4530 N NE2 . GLN B 1 206 ? 15.617  19.368  13.987  1.00 39.86 ? 207 GLN B NE2 1 
ATOM   4531 N N   . GLU B 1 207 ? 16.620  16.716  18.954  1.00 49.54 ? 208 GLU B N   1 
ATOM   4532 C CA  . GLU B 1 207 ? 16.643  17.373  20.283  1.00 53.67 ? 208 GLU B CA  1 
ATOM   4533 C C   . GLU B 1 207 ? 16.760  16.288  21.361  1.00 55.30 ? 208 GLU B C   1 
ATOM   4534 O O   . GLU B 1 207 ? 16.737  16.636  22.548  1.00 54.72 ? 208 GLU B O   1 
ATOM   4535 C CB  . GLU B 1 207 ? 15.410  18.263  20.424  1.00 50.49 ? 208 GLU B CB  1 
ATOM   4536 C CG  . GLU B 1 207 ? 15.159  19.147  19.212  1.00 45.79 ? 208 GLU B CG  1 
ATOM   4537 C CD  . GLU B 1 207 ? 16.221  20.176  18.855  1.00 50.76 ? 208 GLU B CD  1 
ATOM   4538 O OE1 . GLU B 1 207 ? 17.137  20.403  19.668  1.00 54.32 ? 208 GLU B OE1 1 
ATOM   4539 O OE2 . GLU B 1 207 ? 16.127  20.759  17.760  1.00 51.36 ? 208 GLU B OE2 1 
ATOM   4540 N N   . ASN B 1 208 ? 16.906  15.030  20.941  1.00 53.36 ? 209 ASN B N   1 
ATOM   4541 C CA  . ASN B 1 208 ? 16.998  13.892  21.892  1.00 56.17 ? 209 ASN B CA  1 
ATOM   4542 C C   . ASN B 1 208 ? 15.900  14.070  22.938  1.00 58.90 ? 209 ASN B C   1 
ATOM   4543 O O   . ASN B 1 208 ? 16.214  14.075  24.136  1.00 61.75 ? 209 ASN B O   1 
ATOM   4544 C CB  . ASN B 1 208 ? 18.415  13.743  22.445  1.00 58.06 ? 209 ASN B CB  1 
ATOM   4545 C CG  . ASN B 1 208 ? 19.432  13.530  21.345  1.00 65.76 ? 209 ASN B CG  1 
ATOM   4546 O OD1 . ASN B 1 208 ? 19.565  12.425  20.825  1.00 72.40 ? 209 ASN B OD1 1 
ATOM   4547 N ND2 . ASN B 1 208 ? 20.139  14.584  20.969  1.00 67.31 ? 209 ASN B ND2 1 
ATOM   4548 N N   . GLN B 1 209 ? 14.658  14.216  22.477  1.00 58.97 ? 210 GLN B N   1 
ATOM   4549 C CA  . GLN B 1 209 ? 13.521  14.436  23.401  1.00 60.37 ? 210 GLN B CA  1 
ATOM   4550 C C   . GLN B 1 209 ? 12.496  13.312  23.271  1.00 59.51 ? 210 GLN B C   1 
ATOM   4551 O O   . GLN B 1 209 ? 12.465  12.643  22.234  1.00 55.20 ? 210 GLN B O   1 
ATOM   4552 C CB  . GLN B 1 209 ? 12.849  15.772  23.107  1.00 58.80 ? 210 GLN B CB  1 
ATOM   4553 C CG  . GLN B 1 209 ? 13.641  16.970  23.605  1.00 61.69 ? 210 GLN B CG  1 
ATOM   4554 C CD  . GLN B 1 209 ? 12.768  18.172  23.854  1.00 69.98 ? 210 GLN B CD  1 
ATOM   4555 O OE1 . GLN B 1 209 ? 12.284  18.815  22.926  1.00 66.31 ? 210 GLN B OE1 1 
ATOM   4556 N NE2 . GLN B 1 209 ? 12.561  18.487  25.122  1.00 72.40 ? 210 GLN B NE2 1 
ATOM   4557 N N   . PRO B 1 210 ? 11.664  13.079  24.302  1.00 60.87 ? 211 PRO B N   1 
ATOM   4558 C CA  . PRO B 1 210 ? 10.602  12.102  24.208  1.00 64.55 ? 211 PRO B CA  1 
ATOM   4559 C C   . PRO B 1 210 ? 9.320   12.932  24.143  1.00 64.39 ? 211 PRO B C   1 
ATOM   4560 O O   . PRO B 1 210 ? 9.412   14.138  24.127  1.00 62.32 ? 211 PRO B O   1 
ATOM   4561 C CB  . PRO B 1 210 ? 10.539  11.658  25.666  1.00 63.48 ? 211 PRO B CB  1 
ATOM   4562 C CG  . PRO B 1 210 ? 10.716  12.943  26.437  1.00 66.26 ? 211 PRO B CG  1 
ATOM   4563 C CD  . PRO B 1 210 ? 11.724  13.720  25.618  1.00 64.21 ? 211 PRO B CD  1 
ATOM   4564 N N   . ILE B 1 211 ? 8.168   12.292  24.056  1.00 71.08 ? 212 ILE B N   1 
ATOM   4565 C CA  . ILE B 1 211 ? 6.894   13.071  24.092  1.00 72.79 ? 212 ILE B CA  1 
ATOM   4566 C C   . ILE B 1 211 ? 6.397   13.476  25.482  1.00 73.66 ? 212 ILE B C   1 
ATOM   4567 O O   . ILE B 1 211 ? 6.736   14.597  25.908  1.00 77.91 ? 212 ILE B O   1 
ATOM   4568 C CB  . ILE B 1 211 ? 5.843   12.256  23.328  1.00 68.96 ? 212 ILE B CB  1 
ATOM   4569 C CG1 . ILE B 1 211 ? 6.312   11.996  21.903  1.00 66.62 ? 212 ILE B CG1 1 
ATOM   4570 C CG2 . ILE B 1 211 ? 4.494   12.951  23.354  1.00 64.92 ? 212 ILE B CG2 1 
ATOM   4571 C CD1 . ILE B 1 211 ? 6.330   10.550  21.568  1.00 63.14 ? 212 ILE B CD1 1 
ATOM   4572 N N   . GLY B 1 216 ? 5.045   24.281  25.709  1.00 49.98 ? 217 GLY B N   1 
ATOM   4573 C CA  . GLY B 1 216 ? 5.246   25.713  25.533  1.00 46.81 ? 217 GLY B CA  1 
ATOM   4574 C C   . GLY B 1 216 ? 4.101   26.571  26.046  1.00 41.07 ? 217 GLY B C   1 
ATOM   4575 O O   . GLY B 1 216 ? 3.000   26.078  26.277  1.00 40.74 ? 217 GLY B O   1 
ATOM   4576 N N   . PRO B 1 217 ? 4.347   27.870  26.220  1.00 44.79 ? 218 PRO B N   1 
ATOM   4577 C CA  . PRO B 1 217 ? 3.283   28.762  26.713  1.00 40.82 ? 218 PRO B CA  1 
ATOM   4578 C C   . PRO B 1 217 ? 2.154   28.851  25.694  1.00 34.82 ? 218 PRO B C   1 
ATOM   4579 O O   . PRO B 1 217 ? 2.384   29.189  24.530  1.00 39.06 ? 218 PRO B O   1 
ATOM   4580 C CB  . PRO B 1 217 ? 4.001   30.107  26.898  1.00 43.80 ? 218 PRO B CB  1 
ATOM   4581 C CG  . PRO B 1 217 ? 5.170   30.050  25.932  1.00 43.05 ? 218 PRO B CG  1 
ATOM   4582 C CD  . PRO B 1 217 ? 5.583   28.595  25.869  1.00 45.78 ? 218 PRO B CD  1 
ATOM   4583 N N   . LEU B 1 218 ? 0.928   28.536  26.141  1.00 36.01 ? 219 LEU B N   1 
ATOM   4584 C CA  . LEU B 1 218 ? -0.263  28.477  25.294  1.00 36.87 ? 219 LEU B CA  1 
ATOM   4585 C C   . LEU B 1 218 ? 0.046   27.770  23.978  1.00 37.45 ? 219 LEU B C   1 
ATOM   4586 O O   . LEU B 1 218 ? -0.382  28.216  22.908  1.00 34.31 ? 219 LEU B O   1 
ATOM   4587 C CB  . LEU B 1 218 ? -0.825  29.880  25.020  1.00 35.03 ? 219 LEU B CB  1 
ATOM   4588 C CG  . LEU B 1 218 ? -1.467  30.661  26.180  1.00 37.55 ? 219 LEU B CG  1 
ATOM   4589 C CD1 . LEU B 1 218 ? -2.166  31.931  25.680  1.00 39.17 ? 219 LEU B CD1 1 
ATOM   4590 C CD2 . LEU B 1 218 ? -2.438  29.808  26.977  1.00 40.15 ? 219 LEU B CD2 1 
ATOM   4591 N N   . GLY B 1 219 ? 0.794   26.670  24.050  1.00 33.52 ? 220 GLY B N   1 
ATOM   4592 C CA  . GLY B 1 219 ? 1.370   26.080  22.862  1.00 32.66 ? 220 GLY B CA  1 
ATOM   4593 C C   . GLY B 1 219 ? 0.421   25.227  22.048  1.00 35.27 ? 220 GLY B C   1 
ATOM   4594 O O   . GLY B 1 219 ? 0.506   25.225  20.815  1.00 33.90 ? 220 GLY B O   1 
ATOM   4595 N N   . ALA B 1 220 ? -0.477  24.496  22.722  1.00 33.59 ? 221 ALA B N   1 
ATOM   4596 C CA  . ALA B 1 220 ? -1.366  23.546  22.046  1.00 32.93 ? 221 ALA B CA  1 
ATOM   4597 C C   . ALA B 1 220 ? -2.169  24.151  20.897  1.00 31.14 ? 221 ALA B C   1 
ATOM   4598 O O   . ALA B 1 220 ? -2.183  23.551  19.810  1.00 30.60 ? 221 ALA B O   1 
ATOM   4599 C CB  . ALA B 1 220 ? -2.291  22.888  23.082  1.00 32.72 ? 221 ALA B CB  1 
ATOM   4600 N N   . PRO B 1 221 ? -2.839  25.309  21.040  1.00 32.08 ? 222 PRO B N   1 
ATOM   4601 C CA  . PRO B 1 221 ? -3.560  25.876  19.882  1.00 29.98 ? 222 PRO B CA  1 
ATOM   4602 C C   . PRO B 1 221 ? -2.651  26.306  18.734  1.00 27.86 ? 222 PRO B C   1 
ATOM   4603 O O   . PRO B 1 221 ? -3.131  26.427  17.603  1.00 28.44 ? 222 PRO B O   1 
ATOM   4604 C CB  . PRO B 1 221 ? -4.296  27.093  20.474  1.00 32.09 ? 222 PRO B CB  1 
ATOM   4605 C CG  . PRO B 1 221 ? -4.249  26.908  21.968  1.00 34.14 ? 222 PRO B CG  1 
ATOM   4606 C CD  . PRO B 1 221 ? -2.990  26.156  22.242  1.00 34.41 ? 222 PRO B CD  1 
ATOM   4607 N N   . ALA B 1 222 ? -1.364  26.534  18.977  1.00 24.45 ? 223 ALA B N   1 
ATOM   4608 C CA  . ALA B 1 222 ? -0.467  26.998  17.925  1.00 29.03 ? 223 ALA B CA  1 
ATOM   4609 C C   . ALA B 1 222 ? 0.219   25.852  17.188  1.00 28.52 ? 223 ALA B C   1 
ATOM   4610 O O   . ALA B 1 222 ? 0.352   25.908  15.958  1.00 27.48 ? 223 ALA B O   1 
ATOM   4611 C CB  . ALA B 1 222 ? 0.585   27.950  18.511  1.00 27.03 ? 223 ALA B CB  1 
ATOM   4612 N N   . TYR B 1 223 ? 0.644   24.801  17.898  1.00 28.12 ? 224 TYR B N   1 
ATOM   4613 C CA  . TYR B 1 223 ? 1.411   23.748  17.236  1.00 27.40 ? 224 TYR B CA  1 
ATOM   4614 C C   . TYR B 1 223 ? 1.344   22.392  17.930  1.00 27.63 ? 224 TYR B C   1 
ATOM   4615 O O   . TYR B 1 223 ? 2.264   21.584  17.778  1.00 30.58 ? 224 TYR B O   1 
ATOM   4616 C CB  . TYR B 1 223 ? 2.879   24.177  17.114  1.00 27.89 ? 224 TYR B CB  1 
ATOM   4617 C CG  . TYR B 1 223 ? 3.441   24.840  18.356  1.00 31.26 ? 224 TYR B CG  1 
ATOM   4618 C CD1 . TYR B 1 223 ? 3.805   24.090  19.458  1.00 33.49 ? 224 TYR B CD1 1 
ATOM   4619 C CD2 . TYR B 1 223 ? 3.624   26.226  18.412  1.00 31.50 ? 224 TYR B CD2 1 
ATOM   4620 C CE1 . TYR B 1 223 ? 4.330   24.697  20.597  1.00 36.36 ? 224 TYR B CE1 1 
ATOM   4621 C CE2 . TYR B 1 223 ? 4.143   26.838  19.541  1.00 33.58 ? 224 TYR B CE2 1 
ATOM   4622 C CZ  . TYR B 1 223 ? 4.496   26.069  20.632  1.00 34.26 ? 224 TYR B CZ  1 
ATOM   4623 O OH  . TYR B 1 223 ? 5.012   26.660  21.767  1.00 38.62 ? 224 TYR B OH  1 
ATOM   4624 N N   . GLY B 1 224 ? 0.259   22.100  18.638  1.00 27.80 ? 225 GLY B N   1 
ATOM   4625 C CA  . GLY B 1 224 ? 0.209   20.946  19.513  1.00 27.81 ? 225 GLY B CA  1 
ATOM   4626 C C   . GLY B 1 224 ? -0.386  19.638  19.029  1.00 26.47 ? 225 GLY B C   1 
ATOM   4627 O O   . GLY B 1 224 ? -0.453  18.694  19.824  1.00 29.33 ? 225 GLY B O   1 
ATOM   4628 N N   . VAL B 1 225 ? -0.815  19.530  17.763  1.00 25.68 ? 226 VAL B N   1 
ATOM   4629 C CA  . VAL B 1 225 ? -1.588  18.376  17.296  1.00 22.06 ? 226 VAL B CA  1 
ATOM   4630 C C   . VAL B 1 225 ? -0.690  17.426  16.513  1.00 24.38 ? 226 VAL B C   1 
ATOM   4631 O O   . VAL B 1 225 ? 0.189   17.861  15.748  1.00 25.11 ? 226 VAL B O   1 
ATOM   4632 C CB  . VAL B 1 225 ? -2.799  18.812  16.438  1.00 25.87 ? 226 VAL B CB  1 
ATOM   4633 C CG1 . VAL B 1 225 ? -3.641  17.590  16.031  1.00 26.65 ? 226 VAL B CG1 1 
ATOM   4634 C CG2 . VAL B 1 225 ? -3.668  19.812  17.175  1.00 27.60 ? 226 VAL B CG2 1 
ATOM   4635 N N   . LYS B 1 226 ? -0.910  16.119  16.713  1.00 25.47 ? 227 LYS B N   1 
ATOM   4636 C CA  . LYS B 1 226 ? -0.258  15.043  15.977  1.00 25.10 ? 227 LYS B CA  1 
ATOM   4637 C C   . LYS B 1 226 ? -1.330  14.158  15.342  1.00 24.77 ? 227 LYS B C   1 
ATOM   4638 O O   . LYS B 1 226 ? -2.414  13.983  15.908  1.00 25.17 ? 227 LYS B O   1 
ATOM   4639 C CB  . LYS B 1 226 ? 0.650   14.204  16.906  1.00 26.60 ? 227 LYS B CB  1 
ATOM   4640 C CG  . LYS B 1 226 ? 1.706   15.023  17.659  1.00 26.74 ? 227 LYS B CG  1 
ATOM   4641 C CD  . LYS B 1 226 ? 1.159   15.545  18.978  1.00 30.67 ? 227 LYS B CD  1 
ATOM   4642 C CE  . LYS B 1 226 ? 2.177   16.411  19.701  1.00 35.19 ? 227 LYS B CE  1 
ATOM   4643 N NZ  . LYS B 1 226 ? 1.657   16.860  21.021  1.00 34.47 ? 227 LYS B NZ  1 
ATOM   4644 N N   . SER B 1 227 ? -1.046  13.605  14.158  1.00 25.22 ? 228 SER B N   1 
ATOM   4645 C CA  . SER B 1 227 ? -2.092  12.875  13.437  1.00 23.03 ? 228 SER B CA  1 
ATOM   4646 C C   . SER B 1 227 ? -1.478  11.883  12.449  1.00 24.26 ? 228 SER B C   1 
ATOM   4647 O O   . SER B 1 227 ? -0.260  11.856  12.234  1.00 22.43 ? 228 SER B O   1 
ATOM   4648 C CB  . SER B 1 227 ? -3.036  13.857  12.715  1.00 25.71 ? 228 SER B CB  1 
ATOM   4649 O OG  . SER B 1 227 ? -4.181  13.198  12.180  1.00 26.45 ? 228 SER B OG  1 
ATOM   4650 N N   . THR B 1 228 ? -2.349  11.070  11.841  1.00 25.13 ? 229 THR B N   1 
ATOM   4651 C CA  . THR B 1 228 ? -1.986  10.066  10.844  1.00 22.93 ? 229 THR B CA  1 
ATOM   4652 C C   . THR B 1 228 ? -2.420  10.529  9.458   1.00 24.13 ? 229 THR B C   1 
ATOM   4653 O O   . THR B 1 228 ? -3.264  11.411  9.318   1.00 24.66 ? 229 THR B O   1 
ATOM   4654 C CB  . THR B 1 228 ? -2.631  8.701   11.140  1.00 23.77 ? 229 THR B CB  1 
ATOM   4655 O OG1 . THR B 1 228 ? -4.067  8.777   11.001  1.00 21.10 ? 229 THR B OG1 1 
ATOM   4656 C CG2 . THR B 1 228 ? -2.265  8.206   12.541  1.00 23.76 ? 229 THR B CG2 1 
ATOM   4657 N N   . LEU B 1 229 ? -1.833  9.926   8.421   1.00 20.74 ? 230 LEU B N   1 
ATOM   4658 C CA  . LEU B 1 229 ? -2.273  10.236  7.060   1.00 20.76 ? 230 LEU B CA  1 
ATOM   4659 C C   . LEU B 1 229 ? -3.762  9.948   6.839   1.00 23.64 ? 230 LEU B C   1 
ATOM   4660 O O   . LEU B 1 229 ? -4.445  10.805  6.261   1.00 22.11 ? 230 LEU B O   1 
ATOM   4661 C CB  . LEU B 1 229 ? -1.404  9.495   6.031   1.00 20.64 ? 230 LEU B CB  1 
ATOM   4662 C CG  . LEU B 1 229 ? -1.764  9.835   4.577   1.00 22.43 ? 230 LEU B CG  1 
ATOM   4663 C CD1 . LEU B 1 229 ? -1.598  11.364  4.310   1.00 21.27 ? 230 LEU B CD1 1 
ATOM   4664 C CD2 . LEU B 1 229 ? -0.964  9.007   3.566   1.00 22.76 ? 230 LEU B CD2 1 
ATOM   4665 N N   . PRO B 1 230 ? -4.322  8.788   7.223   1.00 25.00 ? 231 PRO B N   1 
ATOM   4666 C CA  . PRO B 1 230 ? -5.766  8.596   6.994   1.00 24.28 ? 231 PRO B CA  1 
ATOM   4667 C C   . PRO B 1 230 ? -6.643  9.623   7.696   1.00 24.56 ? 231 PRO B C   1 
ATOM   4668 O O   . PRO B 1 230 ? -7.656  10.062  7.129   1.00 23.37 ? 231 PRO B O   1 
ATOM   4669 C CB  . PRO B 1 230 ? -6.012  7.171   7.524   1.00 28.21 ? 231 PRO B CB  1 
ATOM   4670 C CG  . PRO B 1 230 ? -4.694  6.490   7.391   1.00 27.23 ? 231 PRO B CG  1 
ATOM   4671 C CD  . PRO B 1 230 ? -3.698  7.550   7.733   1.00 24.48 ? 231 PRO B CD  1 
ATOM   4672 N N   . ASP B 1 231 ? -6.290  10.027  8.919   1.00 23.36 ? 232 ASP B N   1 
ATOM   4673 C CA  . ASP B 1 231 ? -7.064  11.066  9.598   1.00 24.80 ? 232 ASP B CA  1 
ATOM   4674 C C   . ASP B 1 231 ? -6.966  12.404  8.872   1.00 24.50 ? 232 ASP B C   1 
ATOM   4675 O O   . ASP B 1 231 ? -7.968  13.110  8.729   1.00 27.25 ? 232 ASP B O   1 
ATOM   4676 C CB  . ASP B 1 231 ? -6.601  11.237  11.046  1.00 26.07 ? 232 ASP B CB  1 
ATOM   4677 C CG  . ASP B 1 231 ? -7.335  10.301  12.011  1.00 29.94 ? 232 ASP B CG  1 
ATOM   4678 O OD1 . ASP B 1 231 ? -7.985  9.356   11.542  1.00 30.02 ? 232 ASP B OD1 1 
ATOM   4679 O OD2 . ASP B 1 231 ? -7.269  10.517  13.234  1.00 31.20 ? 232 ASP B OD2 1 
ATOM   4680 N N   . MET B 1 232 ? -5.770  12.778  8.421   1.00 22.38 ? 233 MET B N   1 
ATOM   4681 C CA  . MET B 1 232 ? -5.642  14.060  7.734   1.00 21.69 ? 233 MET B CA  1 
ATOM   4682 C C   . MET B 1 232 ? -6.360  14.049  6.387   1.00 23.24 ? 233 MET B C   1 
ATOM   4683 O O   . MET B 1 232 ? -6.905  15.078  5.978   1.00 23.38 ? 233 MET B O   1 
ATOM   4684 C CB  . MET B 1 232 ? -4.165  14.424  7.570   1.00 19.49 ? 233 MET B CB  1 
ATOM   4685 C CG  . MET B 1 232 ? -3.474  14.791  8.900   1.00 21.60 ? 233 MET B CG  1 
ATOM   4686 S SD  . MET B 1 232 ? -4.312  16.041  9.872   1.00 23.67 ? 233 MET B SD  1 
ATOM   4687 C CE  . MET B 1 232 ? -4.120  17.509  8.830   1.00 23.38 ? 233 MET B CE  1 
ATOM   4688 N N   . LEU B 1 233 ? -6.388  12.906  5.690   1.00 20.17 ? 234 LEU B N   1 
ATOM   4689 C CA  . LEU B 1 233 ? -7.193  12.819  4.473   1.00 23.37 ? 234 LEU B CA  1 
ATOM   4690 C C   . LEU B 1 233 ? -8.680  12.909  4.784   1.00 22.88 ? 234 LEU B C   1 
ATOM   4691 O O   . LEU B 1 233 ? -9.443  13.485  3.999   1.00 24.38 ? 234 LEU B O   1 
ATOM   4692 C CB  . LEU B 1 233 ? -6.899  11.524  3.704   1.00 22.78 ? 234 LEU B CB  1 
ATOM   4693 C CG  . LEU B 1 233 ? -5.504  11.459  3.078   1.00 23.36 ? 234 LEU B CG  1 
ATOM   4694 C CD1 . LEU B 1 233 ? -5.259  10.083  2.438   1.00 25.50 ? 234 LEU B CD1 1 
ATOM   4695 C CD2 . LEU B 1 233 ? -5.349  12.562  2.052   1.00 24.85 ? 234 LEU B CD2 1 
ATOM   4696 N N   . SER B 1 234 ? -9.112  12.346  5.918   1.00 20.27 ? 235 SER B N   1 
ATOM   4697 C CA  . SER B 1 234 ? -10.498 12.525  6.347   1.00 22.93 ? 235 SER B CA  1 
ATOM   4698 C C   . SER B 1 234 ? -10.782 13.992  6.654   1.00 23.89 ? 235 SER B C   1 
ATOM   4699 O O   . SER B 1 234 ? -11.857 14.508  6.330   1.00 22.05 ? 235 SER B O   1 
ATOM   4700 C CB  . SER B 1 234 ? -10.798 11.678  7.584   1.00 23.01 ? 235 SER B CB  1 
ATOM   4701 O OG  . SER B 1 234 ? -10.823 10.298  7.291   1.00 30.63 ? 235 SER B OG  1 
ATOM   4702 N N   . PHE B 1 235 ? -9.835  14.673  7.300   1.00 22.79 ? 236 PHE B N   1 
ATOM   4703 C CA  . PHE B 1 235 ? -9.999  16.107  7.540   1.00 20.31 ? 236 PHE B CA  1 
ATOM   4704 C C   . PHE B 1 235 ? -10.132 16.873  6.228   1.00 24.97 ? 236 PHE B C   1 
ATOM   4705 O O   . PHE B 1 235 ? -10.924 17.818  6.128   1.00 26.39 ? 236 PHE B O   1 
ATOM   4706 C CB  . PHE B 1 235 ? -8.821  16.644  8.360   1.00 21.48 ? 236 PHE B CB  1 
ATOM   4707 C CG  . PHE B 1 235 ? -8.946  18.114  8.724   1.00 23.12 ? 236 PHE B CG  1 
ATOM   4708 C CD1 . PHE B 1 235 ? -10.073 18.578  9.384   1.00 23.87 ? 236 PHE B CD1 1 
ATOM   4709 C CD2 . PHE B 1 235 ? -7.923  19.007  8.440   1.00 23.76 ? 236 PHE B CD2 1 
ATOM   4710 C CE1 . PHE B 1 235 ? -10.202 19.932  9.729   1.00 27.34 ? 236 PHE B CE1 1 
ATOM   4711 C CE2 . PHE B 1 235 ? -8.035  20.356  8.782   1.00 27.16 ? 236 PHE B CE2 1 
ATOM   4712 C CZ  . PHE B 1 235 ? -9.184  20.817  9.430   1.00 25.48 ? 236 PHE B CZ  1 
ATOM   4713 N N   . ILE B 1 236 ? -9.364  16.483  5.208   1.00 23.46 ? 237 ILE B N   1 
ATOM   4714 C CA  . ILE B 1 236 ? -9.472  17.166  3.925   1.00 23.65 ? 237 ILE B CA  1 
ATOM   4715 C C   . ILE B 1 236 ? -10.824 16.881  3.287   1.00 24.93 ? 237 ILE B C   1 
ATOM   4716 O O   . ILE B 1 236 ? -11.422 17.759  2.663   1.00 21.38 ? 237 ILE B O   1 
ATOM   4717 C CB  . ILE B 1 236 ? -8.316  16.767  2.993   1.00 23.56 ? 237 ILE B CB  1 
ATOM   4718 C CG1 . ILE B 1 236 ? -6.989  17.314  3.533   1.00 21.56 ? 237 ILE B CG1 1 
ATOM   4719 C CG2 . ILE B 1 236 ? -8.604  17.241  1.555   1.00 25.27 ? 237 ILE B CG2 1 
ATOM   4720 C CD1 . ILE B 1 236 ? -7.005  18.787  3.896   1.00 24.59 ? 237 ILE B CD1 1 
ATOM   4721 N N   . HIS B 1 237 ? -11.317 15.648  3.419   1.00 23.87 ? 238 HIS B N   1 
ATOM   4722 C CA  . HIS B 1 237 ? -12.638 15.312  2.890   1.00 26.66 ? 238 HIS B CA  1 
ATOM   4723 C C   . HIS B 1 237 ? -13.724 16.170  3.523   1.00 27.41 ? 238 HIS B C   1 
ATOM   4724 O O   . HIS B 1 237 ? -14.677 16.577  2.846   1.00 26.70 ? 238 HIS B O   1 
ATOM   4725 C CB  . HIS B 1 237 ? -12.939 13.827  3.117   1.00 27.52 ? 238 HIS B CB  1 
ATOM   4726 C CG  . HIS B 1 237 ? -14.348 13.446  2.784   1.00 27.83 ? 238 HIS B CG  1 
ATOM   4727 N ND1 . HIS B 1 237 ? -15.300 13.213  3.751   1.00 33.66 ? 238 HIS B ND1 1 
ATOM   4728 C CD2 . HIS B 1 237 ? -14.975 13.299  1.593   1.00 32.54 ? 238 HIS B CD2 1 
ATOM   4729 C CE1 . HIS B 1 237 ? -16.450 12.911  3.171   1.00 32.32 ? 238 HIS B CE1 1 
ATOM   4730 N NE2 . HIS B 1 237 ? -16.281 12.962  1.862   1.00 37.90 ? 238 HIS B NE2 1 
ATOM   4731 N N   . ALA B 1 238 ? -13.593 16.463  4.822   1.00 24.81 ? 239 ALA B N   1 
ATOM   4732 C CA  . ALA B 1 238 ? -14.579 17.297  5.506   1.00 27.47 ? 239 ALA B CA  1 
ATOM   4733 C C   . ALA B 1 238 ? -14.522 18.739  5.024   1.00 26.39 ? 239 ALA B C   1 
ATOM   4734 O O   . ALA B 1 238 ? -15.558 19.416  4.970   1.00 25.85 ? 239 ALA B O   1 
ATOM   4735 C CB  . ALA B 1 238 ? -14.360 17.243  7.020   1.00 26.54 ? 239 ALA B CB  1 
ATOM   4736 N N   . ASN B 1 239 ? -13.327 19.226  4.683   1.00 24.56 ? 240 ASN B N   1 
ATOM   4737 C CA  . ASN B 1 239 ? -13.210 20.572  4.126   1.00 23.25 ? 240 ASN B CA  1 
ATOM   4738 C C   . ASN B 1 239 ? -13.703 20.623  2.685   1.00 26.15 ? 240 ASN B C   1 
ATOM   4739 O O   . ASN B 1 239 ? -14.205 21.665  2.245   1.00 28.25 ? 240 ASN B O   1 
ATOM   4740 C CB  . ASN B 1 239 ? -11.761 21.065  4.225   1.00 22.74 ? 240 ASN B CB  1 
ATOM   4741 C CG  . ASN B 1 239 ? -11.463 21.717  5.568   1.00 22.09 ? 240 ASN B CG  1 
ATOM   4742 O OD1 . ASN B 1 239 ? -11.612 22.918  5.724   1.00 26.13 ? 240 ASN B OD1 1 
ATOM   4743 N ND2 . ASN B 1 239 ? -11.076 20.916  6.544   1.00 26.28 ? 240 ASN B ND2 1 
ATOM   4744 N N   . LEU B 1 240 ? -13.586 19.510  1.942   1.00 21.58 ? 241 LEU B N   1 
ATOM   4745 C CA  . LEU B 1 240 ? -14.080 19.458  0.570   1.00 26.26 ? 241 LEU B CA  1 
ATOM   4746 C C   . LEU B 1 240 ? -15.595 19.267  0.507   1.00 26.66 ? 241 LEU B C   1 
ATOM   4747 O O   . LEU B 1 240 ? -16.223 19.661  -0.483  1.00 26.35 ? 241 LEU B O   1 
ATOM   4748 C CB  . LEU B 1 240 ? -13.378 18.328  -0.202  1.00 28.69 ? 241 LEU B CB  1 
ATOM   4749 C CG  . LEU B 1 240 ? -11.952 18.568  -0.745  1.00 26.73 ? 241 LEU B CG  1 
ATOM   4750 C CD1 . LEU B 1 240 ? -11.311 17.252  -1.258  1.00 26.85 ? 241 LEU B CD1 1 
ATOM   4751 C CD2 . LEU B 1 240 ? -11.985 19.614  -1.853  1.00 24.67 ? 241 LEU B CD2 1 
ATOM   4752 N N   . ASN B 1 241 ? -16.199 18.680  1.539   1.00 26.46 ? 242 ASN B N   1 
ATOM   4753 C CA  . ASN B 1 241 ? -17.625 18.333  1.519   1.00 27.70 ? 242 ASN B CA  1 
ATOM   4754 C C   . ASN B 1 241 ? -18.242 18.562  2.888   1.00 28.05 ? 242 ASN B C   1 
ATOM   4755 O O   . ASN B 1 241 ? -18.761 17.637  3.518   1.00 28.78 ? 242 ASN B O   1 
ATOM   4756 C CB  . ASN B 1 241 ? -17.820 16.881  1.083   1.00 35.37 ? 242 ASN B CB  1 
ATOM   4757 C CG  . ASN B 1 241 ? -17.749 16.729  -0.399  1.00 35.73 ? 242 ASN B CG  1 
ATOM   4758 O OD1 . ASN B 1 241 ? -18.686 17.102  -1.112  1.00 41.98 ? 242 ASN B OD1 1 
ATOM   4759 N ND2 . ASN B 1 241 ? -16.618 16.238  -0.890  1.00 35.11 ? 242 ASN B ND2 1 
ATOM   4760 N N   . PRO B 1 242 ? -18.219 19.799  3.373   1.00 27.78 ? 243 PRO B N   1 
ATOM   4761 C CA  . PRO B 1 242 ? -18.783 20.060  4.699   1.00 28.13 ? 243 PRO B CA  1 
ATOM   4762 C C   . PRO B 1 242 ? -20.280 19.828  4.756   1.00 29.60 ? 243 PRO B C   1 
ATOM   4763 O O   . PRO B 1 242 ? -20.818 19.567  5.841   1.00 30.23 ? 243 PRO B O   1 
ATOM   4764 C CB  . PRO B 1 242 ? -18.428 21.530  4.936   1.00 27.65 ? 243 PRO B CB  1 
ATOM   4765 C CG  . PRO B 1 242 ? -18.432 22.101  3.553   1.00 29.73 ? 243 PRO B CG  1 
ATOM   4766 C CD  . PRO B 1 242 ? -17.819 21.037  2.688   1.00 27.44 ? 243 PRO B CD  1 
ATOM   4767 N N   . GLN B 1 243 ? -20.970 19.887  3.620   1.00 30.41 ? 244 GLN B N   1 
ATOM   4768 C CA  . GLN B 1 243 ? -22.415 19.724  3.643   1.00 31.98 ? 244 GLN B CA  1 
ATOM   4769 C C   . GLN B 1 243 ? -22.824 18.280  3.885   1.00 32.60 ? 244 GLN B C   1 
ATOM   4770 O O   . GLN B 1 243 ? -24.019 18.008  4.046   1.00 34.02 ? 244 GLN B O   1 
ATOM   4771 C CB  . GLN B 1 243 ? -23.020 20.245  2.337   1.00 32.82 ? 244 GLN B CB  1 
ATOM   4772 C CG  . GLN B 1 243 ? -22.866 19.321  1.144   1.00 33.01 ? 244 GLN B CG  1 
ATOM   4773 C CD  . GLN B 1 243 ? -21.437 19.164  0.664   1.00 35.26 ? 244 GLN B CD  1 
ATOM   4774 O OE1 . GLN B 1 243 ? -20.530 19.893  1.084   1.00 32.92 ? 244 GLN B OE1 1 
ATOM   4775 N NE2 . GLN B 1 243 ? -21.227 18.199  -0.229  1.00 35.61 ? 244 GLN B NE2 1 
ATOM   4776 N N   . LYS B 1 244 ? -21.865 17.357  3.920   1.00 31.85 ? 245 LYS B N   1 
ATOM   4777 C CA  . LYS B 1 244 ? -22.151 15.971  4.258   1.00 32.44 ? 245 LYS B CA  1 
ATOM   4778 C C   . LYS B 1 244 ? -22.047 15.704  5.753   1.00 32.02 ? 245 LYS B C   1 
ATOM   4779 O O   . LYS B 1 244 ? -22.208 14.558  6.174   1.00 36.27 ? 245 LYS B O   1 
ATOM   4780 C CB  . LYS B 1 244 ? -21.223 15.038  3.473   1.00 31.32 ? 245 LYS B CB  1 
ATOM   4781 C CG  . LYS B 1 244 ? -21.407 15.175  1.971   1.00 32.08 ? 245 LYS B CG  1 
ATOM   4782 C CD  . LYS B 1 244 ? -20.734 14.061  1.197   1.00 34.79 ? 245 LYS B CD  1 
ATOM   4783 C CE  . LYS B 1 244 ? -21.361 13.926  -0.183  1.00 36.63 ? 245 LYS B CE  1 
ATOM   4784 N NZ  . LYS B 1 244 ? -20.671 12.904  -0.997  1.00 41.42 ? 245 LYS B NZ  1 
ATOM   4785 N N   . TYR B 1 245 ? -21.815 16.725  6.557   1.00 31.61 ? 246 TYR B N   1 
ATOM   4786 C CA  . TYR B 1 245 ? -21.645 16.594  7.993   1.00 31.64 ? 246 TYR B CA  1 
ATOM   4787 C C   . TYR B 1 245 ? -22.814 17.219  8.740   1.00 32.83 ? 246 TYR B C   1 
ATOM   4788 O O   . TYR B 1 245 ? -23.546 18.044  8.184   1.00 34.05 ? 246 TYR B O   1 
ATOM   4789 C CB  . TYR B 1 245 ? -20.330 17.257  8.429   1.00 30.10 ? 246 TYR B CB  1 
ATOM   4790 C CG  . TYR B 1 245 ? -19.145 16.450  7.982   1.00 31.28 ? 246 TYR B CG  1 
ATOM   4791 C CD1 . TYR B 1 245 ? -18.821 16.349  6.633   1.00 28.88 ? 246 TYR B CD1 1 
ATOM   4792 C CD2 . TYR B 1 245 ? -18.373 15.743  8.899   1.00 32.39 ? 246 TYR B CD2 1 
ATOM   4793 C CE1 . TYR B 1 245 ? -17.755 15.586  6.213   1.00 29.74 ? 246 TYR B CE1 1 
ATOM   4794 C CE2 . TYR B 1 245 ? -17.290 14.984  8.484   1.00 34.82 ? 246 TYR B CE2 1 
ATOM   4795 C CZ  . TYR B 1 245 ? -16.989 14.907  7.143   1.00 31.35 ? 246 TYR B CZ  1 
ATOM   4796 O OH  . TYR B 1 245 ? -15.924 14.150  6.724   1.00 28.87 ? 246 TYR B OH  1 
ATOM   4797 N N   . PRO B 1 246 ? -23.032 16.829  10.013  1.00 34.71 ? 247 PRO B N   1 
ATOM   4798 C CA  . PRO B 1 246 ? -24.059 17.490  10.826  1.00 37.21 ? 247 PRO B CA  1 
ATOM   4799 C C   . PRO B 1 246 ? -23.856 19.002  10.844  1.00 34.30 ? 247 PRO B C   1 
ATOM   4800 O O   . PRO B 1 246 ? -22.740 19.475  10.611  1.00 34.45 ? 247 PRO B O   1 
ATOM   4801 C CB  . PRO B 1 246 ? -23.862 16.865  12.213  1.00 39.49 ? 247 PRO B CB  1 
ATOM   4802 C CG  . PRO B 1 246 ? -23.249 15.547  11.959  1.00 36.45 ? 247 PRO B CG  1 
ATOM   4803 C CD  . PRO B 1 246 ? -22.412 15.685  10.717  1.00 33.08 ? 247 PRO B CD  1 
ATOM   4804 N N   . ALA B 1 247 ? -24.915 19.763  11.125  1.00 35.27 ? 248 ALA B N   1 
ATOM   4805 C CA  . ALA B 1 247 ? -24.887 21.203  10.873  1.00 38.83 ? 248 ALA B CA  1 
ATOM   4806 C C   . ALA B 1 247 ? -23.874 21.940  11.741  1.00 38.47 ? 248 ALA B C   1 
ATOM   4807 O O   . ALA B 1 247 ? -23.319 22.959  11.310  1.00 39.49 ? 248 ALA B O   1 
ATOM   4808 C CB  . ALA B 1 247 ? -26.279 21.798  11.080  1.00 40.62 ? 248 ALA B CB  1 
ATOM   4809 N N   . ASP B 1 248 ? -23.620 21.468  12.964  1.00 38.17 ? 249 ASP B N   1 
ATOM   4810 C CA  . ASP B 1 248 ? -22.771 22.254  13.858  1.00 37.63 ? 249 ASP B CA  1 
ATOM   4811 C C   . ASP B 1 248 ? -21.304 22.177  13.447  1.00 37.67 ? 249 ASP B C   1 
ATOM   4812 O O   . ASP B 1 248 ? -20.582 23.177  13.532  1.00 37.61 ? 249 ASP B O   1 
ATOM   4813 C CB  . ASP B 1 248 ? -22.931 21.798  15.305  1.00 41.91 ? 249 ASP B CB  1 
ATOM   4814 C CG  . ASP B 1 248 ? -24.304 22.115  15.880  1.00 44.88 ? 249 ASP B CG  1 
ATOM   4815 O OD1 . ASP B 1 248 ? -24.995 23.026  15.376  1.00 45.02 ? 249 ASP B OD1 1 
ATOM   4816 O OD2 . ASP B 1 248 ? -24.683 21.445  16.858  1.00 46.91 ? 249 ASP B OD2 1 
ATOM   4817 N N   . ILE B 1 249 ? -20.836 21.005  13.021  1.00 32.67 ? 250 ILE B N   1 
ATOM   4818 C CA  . ILE B 1 249 ? -19.459 20.925  12.535  1.00 35.03 ? 250 ILE B CA  1 
ATOM   4819 C C   . ILE B 1 249 ? -19.377 21.408  11.089  1.00 31.91 ? 250 ILE B C   1 
ATOM   4820 O O   . ILE B 1 249 ? -18.325 21.891  10.654  1.00 30.15 ? 250 ILE B O   1 
ATOM   4821 C CB  . ILE B 1 249 ? -18.886 19.501  12.702  1.00 34.17 ? 250 ILE B CB  1 
ATOM   4822 C CG1 . ILE B 1 249 ? -17.353 19.505  12.564  1.00 31.72 ? 250 ILE B CG1 1 
ATOM   4823 C CG2 . ILE B 1 249 ? -19.485 18.535  11.689  1.00 29.69 ? 250 ILE B CG2 1 
ATOM   4824 C CD1 . ILE B 1 249 ? -16.632 20.303  13.645  1.00 33.82 ? 250 ILE B CD1 1 
ATOM   4825 N N   . GLN B 1 250 ? -20.478 21.311  10.337  1.00 31.44 ? 251 GLN B N   1 
ATOM   4826 C CA  . GLN B 1 250 ? -20.522 21.876  8.991   1.00 31.66 ? 251 GLN B CA  1 
ATOM   4827 C C   . GLN B 1 250 ? -20.358 23.388  9.035   1.00 31.80 ? 251 GLN B C   1 
ATOM   4828 O O   . GLN B 1 250 ? -19.564 23.959  8.278   1.00 30.05 ? 251 GLN B O   1 
ATOM   4829 C CB  . GLN B 1 250 ? -21.841 21.512  8.292   1.00 34.96 ? 251 GLN B CB  1 
ATOM   4830 C CG  . GLN B 1 250 ? -22.043 22.251  6.947   1.00 31.07 ? 251 GLN B CG  1 
ATOM   4831 C CD  . GLN B 1 250 ? -23.510 22.416  6.567   1.00 41.10 ? 251 GLN B CD  1 
ATOM   4832 O OE1 . GLN B 1 250 ? -23.889 22.243  5.406   1.00 41.45 ? 251 GLN B OE1 1 
ATOM   4833 N NE2 . GLN B 1 250 ? -24.338 22.772  7.544   1.00 44.22 ? 251 GLN B NE2 1 
ATOM   4834 N N   . ARG B 1 251 ? -21.100 24.055  9.926   1.00 32.41 ? 252 ARG B N   1 
ATOM   4835 C CA  . ARG B 1 251 ? -20.959 25.505  10.066  1.00 34.61 ? 252 ARG B CA  1 
ATOM   4836 C C   . ARG B 1 251 ? -19.563 25.888  10.544  1.00 30.93 ? 252 ARG B C   1 
ATOM   4837 O O   . ARG B 1 251 ? -19.006 26.897  10.102  1.00 31.38 ? 252 ARG B O   1 
ATOM   4838 C CB  . ARG B 1 251 ? -22.020 26.063  11.017  1.00 36.35 ? 252 ARG B CB  1 
ATOM   4839 C CG  . ARG B 1 251 ? -23.412 26.144  10.404  1.00 39.99 ? 252 ARG B CG  1 
ATOM   4840 C CD  . ARG B 1 251 ? -24.355 26.961  11.274  1.00 51.35 ? 252 ARG B CD  1 
ATOM   4841 N NE  . ARG B 1 251 ? -25.459 26.153  11.773  1.00 57.53 ? 252 ARG B NE  1 
ATOM   4842 C CZ  . ARG B 1 251 ? -25.497 25.602  12.980  1.00 57.44 ? 252 ARG B CZ  1 
ATOM   4843 N NH1 . ARG B 1 251 ? -24.509 25.771  13.850  1.00 53.36 ? 252 ARG B NH1 1 
ATOM   4844 N NH2 . ARG B 1 251 ? -26.553 24.868  13.325  1.00 51.45 ? 252 ARG B NH2 1 
ATOM   4845 N N   . ALA B 1 252 ? -18.983 25.096  11.449  1.00 31.40 ? 253 ALA B N   1 
ATOM   4846 C CA  . ALA B 1 252 ? -17.617 25.354  11.896  1.00 28.95 ? 253 ALA B CA  1 
ATOM   4847 C C   . ALA B 1 252 ? -16.640 25.323  10.729  1.00 30.14 ? 253 ALA B C   1 
ATOM   4848 O O   . ALA B 1 252 ? -15.781 26.201  10.598  1.00 26.73 ? 253 ALA B O   1 
ATOM   4849 C CB  . ALA B 1 252 ? -17.206 24.328  12.951  1.00 32.88 ? 253 ALA B CB  1 
ATOM   4850 N N   . ILE B 1 253 ? -16.740 24.294  9.883   1.00 26.84 ? 254 ILE B N   1 
ATOM   4851 C CA  . ILE B 1 253 ? -15.805 24.139  8.771   1.00 28.19 ? 254 ILE B CA  1 
ATOM   4852 C C   . ILE B 1 253 ? -15.946 25.297  7.790   1.00 29.21 ? 254 ILE B C   1 
ATOM   4853 O O   . ILE B 1 253 ? -14.950 25.892  7.354   1.00 27.79 ? 254 ILE B O   1 
ATOM   4854 C CB  . ILE B 1 253 ? -16.025 22.779  8.080   1.00 25.52 ? 254 ILE B CB  1 
ATOM   4855 C CG1 . ILE B 1 253 ? -15.569 21.649  9.006   1.00 27.09 ? 254 ILE B CG1 1 
ATOM   4856 C CG2 . ILE B 1 253 ? -15.296 22.738  6.756   1.00 25.65 ? 254 ILE B CG2 1 
ATOM   4857 C CD1 . ILE B 1 253 ? -15.995 20.241  8.563   1.00 25.79 ? 254 ILE B CD1 1 
ATOM   4858 N N   . ASN B 1 254 ? -17.188 25.639  7.433   1.00 27.06 ? 255 ASN B N   1 
ATOM   4859 C CA  . ASN B 1 254 ? -17.415 26.759  6.523   1.00 27.03 ? 255 ASN B CA  1 
ATOM   4860 C C   . ASN B 1 254 ? -16.863 28.063  7.079   1.00 29.37 ? 255 ASN B C   1 
ATOM   4861 O O   . ASN B 1 254 ? -16.417 28.923  6.310   1.00 29.57 ? 255 ASN B O   1 
ATOM   4862 C CB  . ASN B 1 254 ? -18.916 26.905  6.226   1.00 32.00 ? 255 ASN B CB  1 
ATOM   4863 C CG  . ASN B 1 254 ? -19.414 25.850  5.232   1.00 35.56 ? 255 ASN B CG  1 
ATOM   4864 O OD1 . ASN B 1 254 ? -18.679 25.458  4.325   1.00 36.52 ? 255 ASN B OD1 1 
ATOM   4865 N ND2 . ASN B 1 254 ? -20.657 25.396  5.397   1.00 36.64 ? 255 ASN B ND2 1 
ATOM   4866 N N   . GLU B 1 255 ? -16.901 28.237  8.402   1.00 29.93 ? 256 GLU B N   1 
ATOM   4867 C CA  . GLU B 1 255 ? -16.392 29.463  9.003   1.00 29.72 ? 256 GLU B CA  1 
ATOM   4868 C C   . GLU B 1 255 ? -14.902 29.630  8.700   1.00 31.89 ? 256 GLU B C   1 
ATOM   4869 O O   . GLU B 1 255 ? -14.439 30.741  8.408   1.00 28.35 ? 256 GLU B O   1 
ATOM   4870 C CB  . GLU B 1 255 ? -16.669 29.441  10.511  1.00 30.38 ? 256 GLU B CB  1 
ATOM   4871 C CG  . GLU B 1 255 ? -16.715 30.795  11.191  1.00 36.94 ? 256 GLU B CG  1 
ATOM   4872 C CD  . GLU B 1 255 ? -17.897 31.652  10.770  1.00 39.96 ? 256 GLU B CD  1 
ATOM   4873 O OE1 . GLU B 1 255 ? -19.063 31.213  10.934  1.00 38.86 ? 256 GLU B OE1 1 
ATOM   4874 O OE2 . GLU B 1 255 ? -17.657 32.783  10.285  1.00 40.24 ? 256 GLU B OE2 1 
ATOM   4875 N N   . THR B 1 256 ? -14.152 28.519  8.696   1.00 28.15 ? 257 THR B N   1 
ATOM   4876 C CA  . THR B 1 256 ? -12.722 28.526  8.391   1.00 24.21 ? 257 THR B CA  1 
ATOM   4877 C C   . THR B 1 256 ? -12.416 28.780  6.915   1.00 26.19 ? 257 THR B C   1 
ATOM   4878 O O   . THR B 1 256 ? -11.240 28.958  6.578   1.00 25.65 ? 257 THR B O   1 
ATOM   4879 C CB  . THR B 1 256 ? -12.038 27.207  8.814   1.00 29.80 ? 257 THR B CB  1 
ATOM   4880 O OG1 . THR B 1 256 ? -12.291 26.163  7.853   1.00 24.16 ? 257 THR B OG1 1 
ATOM   4881 C CG2 . THR B 1 256 ? -12.496 26.753  10.206  1.00 27.04 ? 257 THR B CG2 1 
ATOM   4882 N N   . HIS B 1 257 ? -13.409 28.807  6.025   1.00 24.42 ? 258 HIS B N   1 
ATOM   4883 C CA  . HIS B 1 257 ? -13.132 29.048  4.609   1.00 24.93 ? 258 HIS B CA  1 
ATOM   4884 C C   . HIS B 1 257 ? -13.366 30.483  4.172   1.00 27.48 ? 258 HIS B C   1 
ATOM   4885 O O   . HIS B 1 257 ? -13.090 30.810  3.009   1.00 27.03 ? 258 HIS B O   1 
ATOM   4886 C CB  . HIS B 1 257 ? -13.987 28.161  3.713   1.00 24.20 ? 258 HIS B CB  1 
ATOM   4887 C CG  . HIS B 1 257 ? -13.724 26.702  3.884   1.00 25.53 ? 258 HIS B CG  1 
ATOM   4888 N ND1 . HIS B 1 257 ? -14.540 25.735  3.334   1.00 28.59 ? 258 HIS B ND1 1 
ATOM   4889 C CD2 . HIS B 1 257 ? -12.746 26.042  4.545   1.00 26.06 ? 258 HIS B CD2 1 
ATOM   4890 C CE1 . HIS B 1 257 ? -14.073 24.539  3.645   1.00 25.91 ? 258 HIS B CE1 1 
ATOM   4891 N NE2 . HIS B 1 257 ? -12.989 24.695  4.385   1.00 25.42 ? 258 HIS B NE2 1 
ATOM   4892 N N   . GLN B 1 258 ? -13.914 31.322  5.033   1.00 26.37 ? 259 GLN B N   1 
ATOM   4893 C CA  . GLN B 1 258 ? -14.223 32.692  4.644   1.00 27.12 ? 259 GLN B CA  1 
ATOM   4894 C C   . GLN B 1 258 ? -12.989 33.571  4.805   1.00 28.18 ? 259 GLN B C   1 
ATOM   4895 O O   . GLN B 1 258 ? -12.442 33.672  5.903   1.00 27.51 ? 259 GLN B O   1 
ATOM   4896 C CB  . GLN B 1 258 ? -15.376 33.223  5.491   1.00 31.24 ? 259 GLN B CB  1 
ATOM   4897 C CG  . GLN B 1 258 ? -15.545 34.731  5.382   1.00 34.51 ? 259 GLN B CG  1 
ATOM   4898 C CD  . GLN B 1 258 ? -16.719 35.246  6.184   1.00 39.17 ? 259 GLN B CD  1 
ATOM   4899 O OE1 . GLN B 1 258 ? -17.395 34.483  6.879   1.00 43.73 ? 259 GLN B OE1 1 
ATOM   4900 N NE2 . GLN B 1 258 ? -16.984 36.543  6.076   1.00 42.14 ? 259 GLN B NE2 1 
ATOM   4901 N N   . GLY B 1 259 ? -12.561 34.219  3.723   1.00 27.75 ? 260 GLY B N   1 
ATOM   4902 C CA  . GLY B 1 259 ? -11.419 35.114  3.816   1.00 30.76 ? 260 GLY B CA  1 
ATOM   4903 C C   . GLY B 1 259 ? -11.775 36.345  4.633   1.00 25.28 ? 260 GLY B C   1 
ATOM   4904 O O   . GLY B 1 259 ? -12.873 36.886  4.524   1.00 26.81 ? 260 GLY B O   1 
ATOM   4905 N N   . ARG B 1 260 ? -10.856 36.753  5.504   1.00 22.76 ? 261 ARG B N   1 
ATOM   4906 C CA  . ARG B 1 260 ? -11.104 37.881  6.408   1.00 22.84 ? 261 ARG B CA  1 
ATOM   4907 C C   . ARG B 1 260 ? -10.406 39.170  5.983   1.00 28.18 ? 261 ARG B C   1 
ATOM   4908 O O   . ARG B 1 260 ? -10.819 40.264  6.413   1.00 23.72 ? 261 ARG B O   1 
ATOM   4909 C CB  . ARG B 1 260 ? -10.671 37.499  7.823   1.00 25.50 ? 261 ARG B CB  1 
ATOM   4910 C CG  . ARG B 1 260 ? -11.232 36.141  8.254   1.00 25.97 ? 261 ARG B CG  1 
ATOM   4911 C CD  . ARG B 1 260 ? -12.767 36.200  8.339   1.00 30.64 ? 261 ARG B CD  1 
ATOM   4912 N NE  . ARG B 1 260 ? -13.358 34.919  8.707   1.00 31.11 ? 261 ARG B NE  1 
ATOM   4913 C CZ  . ARG B 1 260 ? -14.556 34.780  9.261   1.00 32.59 ? 261 ARG B CZ  1 
ATOM   4914 N NH1 . ARG B 1 260 ? -15.301 35.832  9.569   1.00 29.45 ? 261 ARG B NH1 1 
ATOM   4915 N NH2 . ARG B 1 260 ? -15.010 33.558  9.525   1.00 31.82 ? 261 ARG B NH2 1 
ATOM   4916 N N   . TYR B 1 261 ? -9.359  39.065  5.170   1.00 23.71 ? 262 TYR B N   1 
ATOM   4917 C CA  . TYR B 1 261 ? -8.668  40.202  4.566   1.00 25.48 ? 262 TYR B CA  1 
ATOM   4918 C C   . TYR B 1 261 ? -7.686  39.611  3.567   1.00 22.56 ? 262 TYR B C   1 
ATOM   4919 O O   . TYR B 1 261 ? -7.552  38.387  3.458   1.00 22.36 ? 262 TYR B O   1 
ATOM   4920 C CB  . TYR B 1 261 ? -7.956  41.089  5.600   1.00 22.37 ? 262 TYR B CB  1 
ATOM   4921 C CG  . TYR B 1 261 ? -6.905  40.370  6.419   1.00 21.88 ? 262 TYR B CG  1 
ATOM   4922 C CD1 . TYR B 1 261 ? -5.643  40.118  5.900   1.00 21.72 ? 262 TYR B CD1 1 
ATOM   4923 C CD2 . TYR B 1 261 ? -7.174  39.951  7.716   1.00 21.71 ? 262 TYR B CD2 1 
ATOM   4924 C CE1 . TYR B 1 261 ? -4.690  39.450  6.637   1.00 21.39 ? 262 TYR B CE1 1 
ATOM   4925 C CE2 . TYR B 1 261 ? -6.220  39.284  8.470   1.00 22.25 ? 262 TYR B CE2 1 
ATOM   4926 C CZ  . TYR B 1 261 ? -4.977  39.044  7.925   1.00 21.22 ? 262 TYR B CZ  1 
ATOM   4927 O OH  . TYR B 1 261 ? -4.027  38.389  8.664   1.00 21.02 ? 262 TYR B OH  1 
ATOM   4928 N N   . GLN B 1 262 ? -6.998  40.477  2.836   1.00 22.80 ? 263 GLN B N   1 
ATOM   4929 C CA  . GLN B 1 262 ? -5.978  40.004  1.916   1.00 26.13 ? 263 GLN B CA  1 
ATOM   4930 C C   . GLN B 1 262 ? -4.677  40.776  2.079   1.00 23.09 ? 263 GLN B C   1 
ATOM   4931 O O   . GLN B 1 262 ? -4.659  41.956  2.466   1.00 22.91 ? 263 GLN B O   1 
ATOM   4932 C CB  . GLN B 1 262 ? -6.467  40.060  0.454   1.00 28.86 ? 263 GLN B CB  1 
ATOM   4933 C CG  . GLN B 1 262 ? -6.350  41.363  -0.257  1.00 26.96 ? 263 GLN B CG  1 
ATOM   4934 C CD  . GLN B 1 262 ? -7.005  41.320  -1.641  1.00 33.54 ? 263 GLN B CD  1 
ATOM   4935 O OE1 . GLN B 1 262 ? -8.154  41.730  -1.803  1.00 34.98 ? 263 GLN B OE1 1 
ATOM   4936 N NE2 . GLN B 1 262 ? -6.280  40.815  -2.634  1.00 32.71 ? 263 GLN B NE2 1 
ATOM   4937 N N   . VAL B 1 263 ? -3.582  40.071  1.802   1.00 22.68 ? 264 VAL B N   1 
ATOM   4938 C CA  . VAL B 1 263 ? -2.258  40.660  1.648   1.00 22.87 ? 264 VAL B CA  1 
ATOM   4939 C C   . VAL B 1 263 ? -1.776  40.258  0.258   1.00 25.98 ? 264 VAL B C   1 
ATOM   4940 O O   . VAL B 1 263 ? -1.451  39.090  0.025   1.00 25.20 ? 264 VAL B O   1 
ATOM   4941 C CB  . VAL B 1 263 ? -1.283  40.200  2.742   1.00 22.43 ? 264 VAL B CB  1 
ATOM   4942 C CG1 . VAL B 1 263 ? 0.130   40.708  2.471   1.00 23.36 ? 264 VAL B CG1 1 
ATOM   4943 C CG2 . VAL B 1 263 ? -1.734  40.682  4.102   1.00 23.48 ? 264 VAL B CG2 1 
ATOM   4944 N N   . ASN B 1 264 ? -1.765  41.214  -0.679  1.00 28.16 ? 265 ASN B N   1 
ATOM   4945 C CA  . ASN B 1 264 ? -1.442  40.913  -2.076  1.00 29.28 ? 265 ASN B CA  1 
ATOM   4946 C C   . ASN B 1 264 ? -2.345  39.818  -2.645  1.00 30.40 ? 265 ASN B C   1 
ATOM   4947 O O   . ASN B 1 264 ? -3.572  39.980  -2.692  1.00 32.29 ? 265 ASN B O   1 
ATOM   4948 C CB  . ASN B 1 264 ? 0.029   40.510  -2.213  1.00 32.09 ? 265 ASN B CB  1 
ATOM   4949 C CG  . ASN B 1 264 ? 0.970   41.516  -1.571  1.00 37.86 ? 265 ASN B CG  1 
ATOM   4950 O OD1 . ASN B 1 264 ? 0.753   42.720  -1.663  1.00 39.94 ? 265 ASN B OD1 1 
ATOM   4951 N ND2 . ASN B 1 264 ? 2.016   41.023  -0.913  1.00 38.37 ? 265 ASN B ND2 1 
ATOM   4952 N N   . THR B 1 265 ? -1.762  38.686  -3.062  1.00 28.38 ? 266 THR B N   1 
ATOM   4953 C CA  . THR B 1 265 ? -2.535  37.604  -3.672  1.00 28.30 ? 266 THR B CA  1 
ATOM   4954 C C   . THR B 1 265 ? -3.016  36.553  -2.671  1.00 24.85 ? 266 THR B C   1 
ATOM   4955 O O   . THR B 1 265 ? -3.629  35.561  -3.084  1.00 26.82 ? 266 THR B O   1 
ATOM   4956 C CB  . THR B 1 265 ? -1.716  36.900  -4.775  1.00 26.82 ? 266 THR B CB  1 
ATOM   4957 O OG1 . THR B 1 265 ? -0.438  36.490  -4.264  1.00 27.42 ? 266 THR B OG1 1 
ATOM   4958 C CG2 . THR B 1 265 ? -1.507  37.819  -5.978  1.00 32.92 ? 266 THR B CG2 1 
ATOM   4959 N N   . MET B 1 266 ? -2.774  36.735  -1.381  1.00 23.37 ? 267 MET B N   1 
ATOM   4960 C CA  . MET B 1 266 ? -3.139  35.745  -0.371  1.00 22.91 ? 267 MET B CA  1 
ATOM   4961 C C   . MET B 1 266 ? -4.266  36.291  0.494   1.00 25.69 ? 267 MET B C   1 
ATOM   4962 O O   . MET B 1 266 ? -4.192  37.428  0.983   1.00 26.44 ? 267 MET B O   1 
ATOM   4963 C CB  . MET B 1 266 ? -1.926  35.393  0.495   1.00 25.82 ? 267 MET B CB  1 
ATOM   4964 C CG  . MET B 1 266 ? -2.169  34.303  1.536   1.00 26.17 ? 267 MET B CG  1 
ATOM   4965 S SD  . MET B 1 266 ? -0.899  34.352  2.823   1.00 36.10 ? 267 MET B SD  1 
ATOM   4966 C CE  . MET B 1 266 ? -1.715  35.447  4.013   1.00 33.49 ? 267 MET B CE  1 
ATOM   4967 N N   . TYR B 1 267 ? -5.318  35.503  0.661   1.00 22.38 ? 268 TYR B N   1 
ATOM   4968 C CA  . TYR B 1 267 ? -6.406  35.864  1.558   1.00 23.53 ? 268 TYR B CA  1 
ATOM   4969 C C   . TYR B 1 267 ? -6.230  35.094  2.860   1.00 23.30 ? 268 TYR B C   1 
ATOM   4970 O O   . TYR B 1 267 ? -5.931  33.894  2.844   1.00 23.61 ? 268 TYR B O   1 
ATOM   4971 C CB  . TYR B 1 267 ? -7.772  35.548  0.938   1.00 25.17 ? 268 TYR B CB  1 
ATOM   4972 C CG  . TYR B 1 267 ? -8.062  36.299  -0.345  1.00 26.72 ? 268 TYR B CG  1 
ATOM   4973 C CD1 . TYR B 1 267 ? -7.474  35.914  -1.545  1.00 27.69 ? 268 TYR B CD1 1 
ATOM   4974 C CD2 . TYR B 1 267 ? -8.924  37.398  -0.356  1.00 30.84 ? 268 TYR B CD2 1 
ATOM   4975 C CE1 . TYR B 1 267 ? -7.738  36.601  -2.731  1.00 32.96 ? 268 TYR B CE1 1 
ATOM   4976 C CE2 . TYR B 1 267 ? -9.191  38.094  -1.536  1.00 30.07 ? 268 TYR B CE2 1 
ATOM   4977 C CZ  . TYR B 1 267 ? -8.598  37.690  -2.718  1.00 33.74 ? 268 TYR B CZ  1 
ATOM   4978 O OH  . TYR B 1 267 ? -8.868  38.364  -3.892  1.00 38.37 ? 268 TYR B OH  1 
ATOM   4979 N N   . GLN B 1 268 ? -6.416  35.781  3.986   1.00 22.62 ? 269 GLN B N   1 
ATOM   4980 C CA  . GLN B 1 268 ? -6.295  35.159  5.304   1.00 22.56 ? 269 GLN B CA  1 
ATOM   4981 C C   . GLN B 1 268 ? -7.686  34.745  5.770   1.00 23.29 ? 269 GLN B C   1 
ATOM   4982 O O   . GLN B 1 268 ? -8.509  35.601  6.097   1.00 23.83 ? 269 GLN B O   1 
ATOM   4983 C CB  . GLN B 1 268 ? -5.658  36.120  6.310   1.00 21.17 ? 269 GLN B CB  1 
ATOM   4984 C CG  . GLN B 1 268 ? -5.429  35.497  7.690   1.00 22.05 ? 269 GLN B CG  1 
ATOM   4985 C CD  . GLN B 1 268 ? -4.390  34.386  7.663   1.00 21.31 ? 269 GLN B CD  1 
ATOM   4986 O OE1 . GLN B 1 268 ? -3.200  34.639  7.454   1.00 22.82 ? 269 GLN B OE1 1 
ATOM   4987 N NE2 . GLN B 1 268 ? -4.834  33.146  7.877   1.00 20.50 ? 269 GLN B NE2 1 
ATOM   4988 N N   . ALA B 1 269 ? -7.956  33.437  5.780   1.00 22.40 ? 270 ALA B N   1 
ATOM   4989 C CA  . ALA B 1 269 ? -9.141  32.888  6.423   1.00 23.04 ? 270 ALA B CA  1 
ATOM   4990 C C   . ALA B 1 269 ? -8.747  32.465  7.841   1.00 25.47 ? 270 ALA B C   1 
ATOM   4991 O O   . ALA B 1 269 ? -7.621  32.722  8.291   1.00 23.09 ? 270 ALA B O   1 
ATOM   4992 C CB  . ALA B 1 269 ? -9.709  31.730  5.592   1.00 23.46 ? 270 ALA B CB  1 
ATOM   4993 N N   . LEU B 1 270 ? -9.650  31.790  8.559   1.00 23.35 ? 271 LEU B N   1 
ATOM   4994 C CA  . LEU B 1 270 ? -9.312  31.315  9.903   1.00 25.34 ? 271 LEU B CA  1 
ATOM   4995 C C   . LEU B 1 270 ? -8.451  30.071  9.765   1.00 23.73 ? 271 LEU B C   1 
ATOM   4996 O O   . LEU B 1 270 ? -8.928  29.034  9.299   1.00 26.36 ? 271 LEU B O   1 
ATOM   4997 C CB  . LEU B 1 270 ? -10.560 31.002  10.726  1.00 28.14 ? 271 LEU B CB  1 
ATOM   4998 C CG  . LEU B 1 270 ? -11.631 32.029  11.035  1.00 31.25 ? 271 LEU B CG  1 
ATOM   4999 C CD1 . LEU B 1 270 ? -12.746 31.343  11.827  1.00 31.86 ? 271 LEU B CD1 1 
ATOM   5000 C CD2 . LEU B 1 270 ? -11.060 33.214  11.803  1.00 31.72 ? 271 LEU B CD2 1 
ATOM   5001 N N   . GLY B 1 271 ? -7.183  30.158  10.155  1.00 21.89 ? 272 GLY B N   1 
ATOM   5002 C CA  . GLY B 1 271 ? -6.283  29.041  9.956   1.00 23.16 ? 272 GLY B CA  1 
ATOM   5003 C C   . GLY B 1 271 ? -5.790  28.890  8.528   1.00 20.40 ? 272 GLY B C   1 
ATOM   5004 O O   . GLY B 1 271 ? -4.588  28.993  8.273   1.00 20.17 ? 272 GLY B O   1 
ATOM   5005 N N   . TRP B 1 272 ? -6.696  28.654  7.587   1.00 21.14 ? 273 TRP B N   1 
ATOM   5006 C CA  . TRP B 1 272 ? -6.291  28.417  6.201   1.00 20.60 ? 273 TRP B CA  1 
ATOM   5007 C C   . TRP B 1 272 ? -5.796  29.694  5.526   1.00 21.93 ? 273 TRP B C   1 
ATOM   5008 O O   . TRP B 1 272 ? -6.294  30.781  5.791   1.00 22.73 ? 273 TRP B O   1 
ATOM   5009 C CB  . TRP B 1 272 ? -7.469  27.904  5.387   1.00 20.87 ? 273 TRP B CB  1 
ATOM   5010 C CG  . TRP B 1 272 ? -7.946  26.528  5.738   1.00 20.95 ? 273 TRP B CG  1 
ATOM   5011 C CD1 . TRP B 1 272 ? -9.047  26.211  6.477   1.00 22.56 ? 273 TRP B CD1 1 
ATOM   5012 C CD2 . TRP B 1 272 ? -7.372  25.286  5.307   1.00 20.76 ? 273 TRP B CD2 1 
ATOM   5013 N NE1 . TRP B 1 272 ? -9.181  24.841  6.558   1.00 21.36 ? 273 TRP B NE1 1 
ATOM   5014 C CE2 . TRP B 1 272 ? -8.159  24.253  5.855   1.00 21.03 ? 273 TRP B CE2 1 
ATOM   5015 C CE3 . TRP B 1 272 ? -6.254  24.953  4.530   1.00 20.49 ? 273 TRP B CE3 1 
ATOM   5016 C CZ2 . TRP B 1 272 ? -7.881  22.896  5.638   1.00 21.61 ? 273 TRP B CZ2 1 
ATOM   5017 C CZ3 . TRP B 1 272 ? -5.970  23.590  4.316   1.00 20.39 ? 273 TRP B CZ3 1 
ATOM   5018 C CH2 . TRP B 1 272 ? -6.784  22.589  4.879   1.00 20.56 ? 273 TRP B CH2 1 
ATOM   5019 N N   . GLU B 1 273 ? -4.835  29.542  4.617   1.00 20.45 ? 274 GLU B N   1 
ATOM   5020 C CA  . GLU B 1 273 ? -4.544  30.572  3.624   1.00 21.55 ? 274 GLU B CA  1 
ATOM   5021 C C   . GLU B 1 273 ? -5.352  30.261  2.378   1.00 21.80 ? 274 GLU B C   1 
ATOM   5022 O O   . GLU B 1 273 ? -5.460  29.106  1.975   1.00 21.08 ? 274 GLU B O   1 
ATOM   5023 C CB  . GLU B 1 273 ? -3.050  30.622  3.289   1.00 22.39 ? 274 GLU B CB  1 
ATOM   5024 C CG  . GLU B 1 273 ? -2.210  31.025  4.462   1.00 22.59 ? 274 GLU B CG  1 
ATOM   5025 C CD  . GLU B 1 273 ? -0.721  31.074  4.157   1.00 34.22 ? 274 GLU B CD  1 
ATOM   5026 O OE1 . GLU B 1 273 ? -0.305  30.649  3.051   1.00 30.47 ? 274 GLU B OE1 1 
ATOM   5027 O OE2 . GLU B 1 273 ? 0.037   31.537  5.039   1.00 37.63 ? 274 GLU B OE2 1 
ATOM   5028 N N   . GLU B 1 274 ? -5.917  31.298  1.770   1.00 22.06 ? 275 GLU B N   1 
ATOM   5029 C CA  . GLU B 1 274 ? -6.870  31.154  0.690   1.00 23.40 ? 275 GLU B CA  1 
ATOM   5030 C C   . GLU B 1 274 ? -6.378  31.904  -0.543  1.00 24.89 ? 275 GLU B C   1 
ATOM   5031 O O   . GLU B 1 274 ? -5.764  32.975  -0.427  1.00 22.99 ? 275 GLU B O   1 
ATOM   5032 C CB  . GLU B 1 274 ? -8.237  31.674  1.148   1.00 24.93 ? 275 GLU B CB  1 
ATOM   5033 C CG  . GLU B 1 274 ? -9.259  31.849  0.049   1.00 25.98 ? 275 GLU B CG  1 
ATOM   5034 C CD  . GLU B 1 274 ? -10.500 32.583  0.521   1.00 33.65 ? 275 GLU B CD  1 
ATOM   5035 O OE1 . GLU B 1 274 ? -11.394 32.822  -0.313  1.00 41.15 ? 275 GLU B OE1 1 
ATOM   5036 O OE2 . GLU B 1 274 ? -10.596 32.929  1.717   1.00 31.73 ? 275 GLU B OE2 1 
ATOM   5037 N N   . PHE B 1 275 ? -6.656  31.335  -1.725  1.00 23.06 ? 276 PHE B N   1 
ATOM   5038 C CA  . PHE B 1 275 ? -6.256  31.922  -3.000  1.00 23.73 ? 276 PHE B CA  1 
ATOM   5039 C C   . PHE B 1 275 ? -7.358  31.761  -4.040  1.00 26.47 ? 276 PHE B C   1 
ATOM   5040 O O   . PHE B 1 275 ? -8.127  30.791  -4.015  1.00 24.79 ? 276 PHE B O   1 
ATOM   5041 C CB  . PHE B 1 275 ? -4.979  31.276  -3.535  1.00 24.11 ? 276 PHE B CB  1 
ATOM   5042 C CG  . PHE B 1 275 ? -3.887  31.171  -2.509  1.00 23.33 ? 276 PHE B CG  1 
ATOM   5043 C CD1 . PHE B 1 275 ? -3.806  30.063  -1.688  1.00 22.27 ? 276 PHE B CD1 1 
ATOM   5044 C CD2 . PHE B 1 275 ? -2.966  32.189  -2.352  1.00 23.07 ? 276 PHE B CD2 1 
ATOM   5045 C CE1 . PHE B 1 275 ? -2.811  29.965  -0.732  1.00 22.04 ? 276 PHE B CE1 1 
ATOM   5046 C CE2 . PHE B 1 275 ? -1.953  32.101  -1.396  1.00 24.75 ? 276 PHE B CE2 1 
ATOM   5047 C CZ  . PHE B 1 275 ? -1.887  30.978  -0.582  1.00 25.26 ? 276 PHE B CZ  1 
ATOM   5048 N N   . SER B 1 276 ? -7.416  32.724  -4.963  1.00 25.27 ? 277 SER B N   1 
ATOM   5049 C CA  . SER B 1 276 ? -8.247  32.574  -6.150  1.00 26.28 ? 277 SER B CA  1 
ATOM   5050 C C   . SER B 1 276 ? -7.750  31.406  -6.997  1.00 28.77 ? 277 SER B C   1 
ATOM   5051 O O   . SER B 1 276 ? -6.546  31.246  -7.215  1.00 28.33 ? 277 SER B O   1 
ATOM   5052 C CB  . SER B 1 276 ? -8.226  33.852  -6.982  1.00 27.13 ? 277 SER B CB  1 
ATOM   5053 O OG  . SER B 1 276 ? -8.982  33.652  -8.156  1.00 29.26 ? 277 SER B OG  1 
ATOM   5054 N N   . TYR B 1 277 ? -8.684  30.589  -7.482  1.00 30.40 ? 278 TYR B N   1 
ATOM   5055 C CA  . TYR B 1 277 ? -8.330  29.406  -8.256  1.00 30.58 ? 278 TYR B CA  1 
ATOM   5056 C C   . TYR B 1 277 ? -8.796  29.558  -9.692  1.00 31.80 ? 278 TYR B C   1 
ATOM   5057 O O   . TYR B 1 277 ? -9.961  29.911  -9.918  1.00 31.90 ? 278 TYR B O   1 
ATOM   5058 C CB  . TYR B 1 277 ? -8.945  28.141  -7.655  1.00 30.66 ? 278 TYR B CB  1 
ATOM   5059 C CG  . TYR B 1 277 ? -8.637  26.907  -8.481  1.00 33.10 ? 278 TYR B CG  1 
ATOM   5060 C CD1 . TYR B 1 277 ? -7.439  26.217  -8.307  1.00 29.22 ? 278 TYR B CD1 1 
ATOM   5061 C CD2 . TYR B 1 277 ? -9.524  26.450  -9.453  1.00 33.28 ? 278 TYR B CD2 1 
ATOM   5062 C CE1 . TYR B 1 277 ? -7.136  25.096  -9.064  1.00 35.74 ? 278 TYR B CE1 1 
ATOM   5063 C CE2 . TYR B 1 277 ? -9.226  25.317  -10.217 1.00 36.25 ? 278 TYR B CE2 1 
ATOM   5064 C CZ  . TYR B 1 277 ? -8.028  24.651  -10.015 1.00 35.23 ? 278 TYR B CZ  1 
ATOM   5065 O OH  . TYR B 1 277 ? -7.714  23.530  -10.756 1.00 38.75 ? 278 TYR B OH  1 
ATOM   5066 N N   . PRO B 1 278 ? -7.951  29.244  -10.685 1.00 31.89 ? 279 PRO B N   1 
ATOM   5067 C CA  . PRO B 1 278 ? -6.608  28.654  -10.563 1.00 34.47 ? 279 PRO B CA  1 
ATOM   5068 C C   . PRO B 1 278 ? -5.563  29.635  -10.046 1.00 33.67 ? 279 PRO B C   1 
ATOM   5069 O O   . PRO B 1 278 ? -5.600  30.825  -10.354 1.00 28.53 ? 279 PRO B O   1 
ATOM   5070 C CB  . PRO B 1 278 ? -6.310  28.186  -11.996 1.00 36.92 ? 279 PRO B CB  1 
ATOM   5071 C CG  . PRO B 1 278 ? -7.085  29.145  -12.865 1.00 39.63 ? 279 PRO B CG  1 
ATOM   5072 C CD  . PRO B 1 278 ? -8.350  29.428  -12.094 1.00 33.83 ? 279 PRO B CD  1 
ATOM   5073 N N   . ALA B 1 279 ? -4.631  29.142  -9.234  1.00 29.67 ? 280 ALA B N   1 
ATOM   5074 C CA  . ALA B 1 279 ? -3.532  29.935  -8.707  1.00 29.75 ? 280 ALA B CA  1 
ATOM   5075 C C   . ALA B 1 279 ? -2.236  29.522  -9.388  1.00 33.69 ? 280 ALA B C   1 
ATOM   5076 O O   . ALA B 1 279 ? -2.005  28.333  -9.635  1.00 31.44 ? 280 ALA B O   1 
ATOM   5077 C CB  . ALA B 1 279 ? -3.399  29.760  -7.189  1.00 28.49 ? 280 ALA B CB  1 
ATOM   5078 N N   . THR B 1 280 ? -1.395  30.502  -9.707  1.00 28.31 ? 281 THR B N   1 
ATOM   5079 C CA  . THR B 1 280 ? -0.096  30.152  -10.255 1.00 31.79 ? 281 THR B CA  1 
ATOM   5080 C C   . THR B 1 280 ? 0.791   29.579  -9.158  1.00 32.41 ? 281 THR B C   1 
ATOM   5081 O O   . THR B 1 280 ? 0.557   29.787  -7.960  1.00 27.63 ? 281 THR B O   1 
ATOM   5082 C CB  . THR B 1 280 ? 0.584   31.366  -10.888 1.00 30.96 ? 281 THR B CB  1 
ATOM   5083 O OG1 . THR B 1 280 ? 0.792   32.380  -9.891  1.00 29.51 ? 281 THR B OG1 1 
ATOM   5084 C CG2 . THR B 1 280 ? -0.266  31.910  -12.026 1.00 32.81 ? 281 THR B CG2 1 
ATOM   5085 N N   . LEU B 1 281 ? 1.818   28.836  -9.581  1.00 32.13 ? 282 LEU B N   1 
ATOM   5086 C CA  . LEU B 1 281 ? 2.801   28.345  -8.620  1.00 30.12 ? 282 LEU B CA  1 
ATOM   5087 C C   . LEU B 1 281 ? 3.445   29.501  -7.859  1.00 28.40 ? 282 LEU B C   1 
ATOM   5088 O O   . LEU B 1 281 ? 3.630   29.421  -6.640  1.00 26.63 ? 282 LEU B O   1 
ATOM   5089 C CB  . LEU B 1 281 ? 3.858   27.501  -9.332  1.00 31.34 ? 282 LEU B CB  1 
ATOM   5090 C CG  . LEU B 1 281 ? 4.997   26.947  -8.475  1.00 30.09 ? 282 LEU B CG  1 
ATOM   5091 C CD1 . LEU B 1 281 ? 4.458   26.056  -7.332  1.00 25.30 ? 282 LEU B CD1 1 
ATOM   5092 C CD2 . LEU B 1 281 ? 5.993   26.183  -9.349  1.00 30.11 ? 282 LEU B CD2 1 
ATOM   5093 N N   . GLN B 1 282 ? 3.754   30.606  -8.554  1.00 28.43 ? 283 GLN B N   1 
ATOM   5094 C CA  . GLN B 1 282 ? 4.436   31.725  -7.903  1.00 29.13 ? 283 GLN B CA  1 
ATOM   5095 C C   . GLN B 1 282 ? 3.563   32.365  -6.831  1.00 28.88 ? 283 GLN B C   1 
ATOM   5096 O O   . GLN B 1 282 ? 4.071   32.812  -5.795  1.00 27.91 ? 283 GLN B O   1 
ATOM   5097 C CB  . GLN B 1 282 ? 4.858   32.773  -8.940  1.00 33.88 ? 283 GLN B CB  1 
ATOM   5098 C CG  . GLN B 1 282 ? 5.860   33.792  -8.407  1.00 32.12 ? 283 GLN B CG  1 
ATOM   5099 C CD  . GLN B 1 282 ? 7.135   33.134  -7.905  1.00 37.06 ? 283 GLN B CD  1 
ATOM   5100 O OE1 . GLN B 1 282 ? 7.488   33.246  -6.729  1.00 36.00 ? 283 GLN B OE1 1 
ATOM   5101 N NE2 . GLN B 1 282 ? 7.825   32.432  -8.794  1.00 36.43 ? 283 GLN B NE2 1 
ATOM   5102 N N   . THR B 1 283 ? 2.254   32.451  -7.081  1.00 26.36 ? 284 THR B N   1 
ATOM   5103 C CA  . THR B 1 283 ? 1.328   32.943  -6.066  1.00 25.78 ? 284 THR B CA  1 
ATOM   5104 C C   . THR B 1 283 ? 1.382   32.077  -4.815  1.00 27.39 ? 284 THR B C   1 
ATOM   5105 O O   . THR B 1 283 ? 1.433   32.590  -3.689  1.00 26.08 ? 284 THR B O   1 
ATOM   5106 C CB  . THR B 1 283 ? -0.091  32.974  -6.639  1.00 28.62 ? 284 THR B CB  1 
ATOM   5107 O OG1 . THR B 1 283 ? -0.161  33.972  -7.664  1.00 28.96 ? 284 THR B OG1 1 
ATOM   5108 C CG2 . THR B 1 283 ? -1.131  33.277  -5.548  1.00 26.07 ? 284 THR B CG2 1 
ATOM   5109 N N   . LEU B 1 284 ? 1.379   30.759  -4.994  1.00 24.23 ? 285 LEU B N   1 
ATOM   5110 C CA  . LEU B 1 284 ? 1.427   29.870  -3.841  1.00 24.63 ? 285 LEU B CA  1 
ATOM   5111 C C   . LEU B 1 284 ? 2.763   29.975  -3.122  1.00 24.85 ? 285 LEU B C   1 
ATOM   5112 O O   . LEU B 1 284 ? 2.808   29.940  -1.884  1.00 24.85 ? 285 LEU B O   1 
ATOM   5113 C CB  . LEU B 1 284 ? 1.163   28.426  -4.272  1.00 23.28 ? 285 LEU B CB  1 
ATOM   5114 C CG  . LEU B 1 284 ? -0.201  28.171  -4.915  1.00 27.39 ? 285 LEU B CG  1 
ATOM   5115 C CD1 . LEU B 1 284 ? -0.377  26.680  -5.274  1.00 27.03 ? 285 LEU B CD1 1 
ATOM   5116 C CD2 . LEU B 1 284 ? -1.285  28.631  -3.967  1.00 23.75 ? 285 LEU B CD2 1 
ATOM   5117 N N   . LEU B 1 285 ? 3.859   30.105  -3.881  1.00 24.67 ? 286 LEU B N   1 
ATOM   5118 C CA  . LEU B 1 285 ? 5.177   30.219  -3.261  1.00 26.13 ? 286 LEU B CA  1 
ATOM   5119 C C   . LEU B 1 285 ? 5.322   31.545  -2.514  1.00 29.25 ? 286 LEU B C   1 
ATOM   5120 O O   . LEU B 1 285 ? 5.949   31.602  -1.444  1.00 30.13 ? 286 LEU B O   1 
ATOM   5121 C CB  . LEU B 1 285 ? 6.271   30.074  -4.323  1.00 24.94 ? 286 LEU B CB  1 
ATOM   5122 C CG  . LEU B 1 285 ? 6.487   28.694  -4.972  1.00 26.04 ? 286 LEU B CG  1 
ATOM   5123 C CD1 . LEU B 1 285 ? 7.393   28.817  -6.194  1.00 27.70 ? 286 LEU B CD1 1 
ATOM   5124 C CD2 . LEU B 1 285 ? 7.067   27.684  -3.976  1.00 25.05 ? 286 LEU B CD2 1 
ATOM   5125 N N   . ASP B 1 286 ? 4.745   32.618  -3.062  1.00 27.08 ? 287 ASP B N   1 
ATOM   5126 C CA  . ASP B 1 286 ? 4.861   33.935  -2.430  1.00 26.68 ? 287 ASP B CA  1 
ATOM   5127 C C   . ASP B 1 286 ? 4.189   33.968  -1.066  1.00 28.34 ? 287 ASP B C   1 
ATOM   5128 O O   . ASP B 1 286 ? 4.603   34.736  -0.191  1.00 26.81 ? 287 ASP B O   1 
ATOM   5129 C CB  . ASP B 1 286 ? 4.272   35.009  -3.340  1.00 29.44 ? 287 ASP B CB  1 
ATOM   5130 C CG  . ASP B 1 286 ? 5.176   35.334  -4.522  1.00 35.18 ? 287 ASP B CG  1 
ATOM   5131 O OD1 . ASP B 1 286 ? 6.383   35.016  -4.458  1.00 37.81 ? 287 ASP B OD1 1 
ATOM   5132 O OD2 . ASP B 1 286 ? 4.689   35.919  -5.513  1.00 39.56 ? 287 ASP B OD2 1 
ATOM   5133 N N   . SER B 1 287 ? 3.175   33.127  -0.847  1.00 25.25 ? 288 SER B N   1 
ATOM   5134 C CA  . SER B 1 287 ? 2.531   33.094  0.461   1.00 27.88 ? 288 SER B CA  1 
ATOM   5135 C C   . SER B 1 287 ? 3.504   32.665  1.556   1.00 29.31 ? 288 SER B C   1 
ATOM   5136 O O   . SER B 1 287 ? 3.324   33.029  2.723   1.00 28.80 ? 288 SER B O   1 
ATOM   5137 C CB  . SER B 1 287 ? 1.325   32.153  0.432   1.00 25.57 ? 288 SER B CB  1 
ATOM   5138 O OG  . SER B 1 287 ? 1.750   30.789  0.426   1.00 23.60 ? 288 SER B OG  1 
ATOM   5139 N N   . ASN B 1 288 ? 4.543   31.905  1.202   1.00 27.86 ? 289 ASN B N   1 
ATOM   5140 C CA  . ASN B 1 288 ? 5.500   31.378  2.169   1.00 25.60 ? 289 ASN B CA  1 
ATOM   5141 C C   . ASN B 1 288 ? 6.839   32.118  2.121   1.00 27.46 ? 289 ASN B C   1 
ATOM   5142 O O   . ASN B 1 288 ? 7.841   31.629  2.654   1.00 27.32 ? 289 ASN B O   1 
ATOM   5143 C CB  . ASN B 1 288 ? 5.682   29.868  1.942   1.00 26.55 ? 289 ASN B CB  1 
ATOM   5144 C CG  . ASN B 1 288 ? 4.596   29.018  2.635   1.00 31.09 ? 289 ASN B CG  1 
ATOM   5145 O OD1 . ASN B 1 288 ? 4.915   28.148  3.452   1.00 32.73 ? 289 ASN B OD1 1 
ATOM   5146 N ND2 . ASN B 1 288 ? 3.315   29.268  2.311   1.00 25.02 ? 289 ASN B ND2 1 
ATOM   5147 N N   . SER B 1 289 ? 6.872   33.297  1.504   1.00 28.17 ? 290 SER B N   1 
ATOM   5148 C CA  . SER B 1 289 ? 8.056   34.150  1.514   1.00 29.52 ? 290 SER B CA  1 
ATOM   5149 C C   . SER B 1 289 ? 8.408   34.614  2.930   1.00 28.97 ? 290 SER B C   1 
ATOM   5150 O O   . SER B 1 289 ? 7.558   34.716  3.817   1.00 26.85 ? 290 SER B O   1 
ATOM   5151 C CB  . SER B 1 289 ? 7.835   35.383  0.640   1.00 29.11 ? 290 SER B CB  1 
ATOM   5152 O OG  . SER B 1 289 ? 6.945   36.308  1.264   1.00 30.99 ? 290 SER B OG  1 
ATOM   5153 N N   . GLU B 1 290 ? 9.692   34.930  3.124   1.00 27.32 ? 291 GLU B N   1 
ATOM   5154 C CA  . GLU B 1 290 ? 10.128  35.488  4.402   1.00 30.17 ? 291 GLU B CA  1 
ATOM   5155 C C   . GLU B 1 290 ? 9.345   36.754  4.750   1.00 30.22 ? 291 GLU B C   1 
ATOM   5156 O O   . GLU B 1 290 ? 9.012   36.986  5.917   1.00 32.10 ? 291 GLU B O   1 
ATOM   5157 C CB  . GLU B 1 290 ? 11.634  35.777  4.355   1.00 33.76 ? 291 GLU B CB  1 
ATOM   5158 C CG  . GLU B 1 290 ? 12.194  36.508  5.582   1.00 42.53 ? 291 GLU B CG  1 
ATOM   5159 C CD  . GLU B 1 290 ? 12.365  35.600  6.798   1.00 50.61 ? 291 GLU B CD  1 
ATOM   5160 O OE1 . GLU B 1 290 ? 12.031  34.393  6.702   1.00 55.70 ? 291 GLU B OE1 1 
ATOM   5161 O OE2 . GLU B 1 290 ? 12.852  36.093  7.845   1.00 54.01 ? 291 GLU B OE2 1 
ATOM   5162 N N   . GLN B 1 291 ? 9.030   37.579  3.748   1.00 29.53 ? 292 GLN B N   1 
ATOM   5163 C CA  . GLN B 1 291 ? 8.259   38.795  4.002   1.00 29.63 ? 292 GLN B CA  1 
ATOM   5164 C C   . GLN B 1 291 ? 6.887   38.482  4.608   1.00 28.17 ? 292 GLN B C   1 
ATOM   5165 O O   . GLN B 1 291 ? 6.440   39.162  5.541   1.00 23.79 ? 292 GLN B O   1 
ATOM   5166 C CB  . GLN B 1 291 ? 8.095   39.579  2.705   1.00 27.41 ? 292 GLN B CB  1 
ATOM   5167 C CG  . GLN B 1 291 ? 7.262   40.842  2.870   1.00 30.96 ? 292 GLN B CG  1 
ATOM   5168 C CD  . GLN B 1 291 ? 7.986   41.916  3.653   1.00 30.52 ? 292 GLN B CD  1 
ATOM   5169 O OE1 . GLN B 1 291 ? 9.219   41.997  3.628   1.00 31.92 ? 292 GLN B OE1 1 
ATOM   5170 N NE2 . GLN B 1 291 ? 7.223   42.754  4.356   1.00 26.89 ? 292 GLN B NE2 1 
ATOM   5171 N N   . ILE B 1 292 ? 6.202   37.460  4.095   1.00 25.41 ? 293 ILE B N   1 
ATOM   5172 C CA  . ILE B 1 292 ? 4.873   37.147  4.626   1.00 26.72 ? 293 ILE B CA  1 
ATOM   5173 C C   . ILE B 1 292 ? 4.977   36.460  5.982   1.00 28.96 ? 293 ILE B C   1 
ATOM   5174 O O   . ILE B 1 292 ? 4.182   36.731  6.891   1.00 26.73 ? 293 ILE B O   1 
ATOM   5175 C CB  . ILE B 1 292 ? 4.074   36.293  3.627   1.00 27.89 ? 293 ILE B CB  1 
ATOM   5176 C CG1 . ILE B 1 292 ? 3.760   37.108  2.383   1.00 29.14 ? 293 ILE B CG1 1 
ATOM   5177 C CG2 . ILE B 1 292 ? 2.767   35.799  4.260   1.00 28.58 ? 293 ILE B CG2 1 
ATOM   5178 C CD1 . ILE B 1 292 ? 3.015   38.389  2.674   1.00 30.53 ? 293 ILE B CD1 1 
ATOM   5179 N N   . PHE B 1 293 ? 5.975   35.591  6.147   1.00 26.74 ? 294 PHE B N   1 
ATOM   5180 C CA  . PHE B 1 293 ? 6.090   34.762  7.341   1.00 28.05 ? 294 PHE B CA  1 
ATOM   5181 C C   . PHE B 1 293 ? 6.632   35.536  8.542   1.00 32.48 ? 294 PHE B C   1 
ATOM   5182 O O   . PHE B 1 293 ? 6.146   35.353  9.665   1.00 30.82 ? 294 PHE B O   1 
ATOM   5183 C CB  . PHE B 1 293 ? 6.983   33.556  7.029   1.00 32.87 ? 294 PHE B CB  1 
ATOM   5184 C CG  . PHE B 1 293 ? 7.179   32.627  8.186   1.00 38.74 ? 294 PHE B CG  1 
ATOM   5185 C CD1 . PHE B 1 293 ? 6.192   31.717  8.541   1.00 36.70 ? 294 PHE B CD1 1 
ATOM   5186 C CD2 . PHE B 1 293 ? 8.356   32.660  8.921   1.00 42.71 ? 294 PHE B CD2 1 
ATOM   5187 C CE1 . PHE B 1 293 ? 6.379   30.848  9.620   1.00 43.44 ? 294 PHE B CE1 1 
ATOM   5188 C CE2 . PHE B 1 293 ? 8.557   31.800  10.000  1.00 44.46 ? 294 PHE B CE2 1 
ATOM   5189 C CZ  . PHE B 1 293 ? 7.566   30.892  10.351  1.00 46.37 ? 294 PHE B CZ  1 
ATOM   5190 N N   . MET B 1 294 ? 7.640   36.395  8.342   1.00 29.16 ? 295 MET B N   1 
ATOM   5191 C CA  . MET B 1 294 ? 8.386   36.950  9.466   1.00 31.57 ? 295 MET B CA  1 
ATOM   5192 C C   . MET B 1 294 ? 8.172   38.439  9.706   1.00 29.44 ? 295 MET B C   1 
ATOM   5193 O O   . MET B 1 294 ? 8.564   38.925  10.771  1.00 30.75 ? 295 MET B O   1 
ATOM   5194 C CB  . MET B 1 294 ? 9.899   36.703  9.291   1.00 36.95 ? 295 MET B CB  1 
ATOM   5195 C CG  . MET B 1 294 ? 10.394  35.272  9.559   1.00 46.69 ? 295 MET B CG  1 
ATOM   5196 S SD  . MET B 1 294 ? 10.326  34.630  11.262  1.00 54.92 ? 295 MET B SD  1 
ATOM   5197 C CE  . MET B 1 294 ? 10.740  36.066  12.254  1.00 42.88 ? 295 MET B CE  1 
ATOM   5198 N N   . LYS B 1 295 ? 7.582   39.176  8.769   1.00 27.21 ? 296 LYS B N   1 
ATOM   5199 C CA  . LYS B 1 295 ? 7.490   40.625  8.861   1.00 25.54 ? 296 LYS B CA  1 
ATOM   5200 C C   . LYS B 1 295 ? 6.039   41.076  8.977   1.00 25.17 ? 296 LYS B C   1 
ATOM   5201 O O   . LYS B 1 295 ? 5.116   40.343  8.598   1.00 23.38 ? 296 LYS B O   1 
ATOM   5202 C CB  . LYS B 1 295 ? 8.155   41.277  7.637   1.00 24.74 ? 296 LYS B CB  1 
ATOM   5203 C CG  . LYS B 1 295 ? 9.635   40.907  7.507   1.00 28.77 ? 296 LYS B CG  1 
ATOM   5204 C CD  . LYS B 1 295 ? 10.450  42.012  6.877   1.00 39.94 ? 296 LYS B CD  1 
ATOM   5205 C CE  . LYS B 1 295 ? 11.945  41.692  6.974   1.00 42.65 ? 296 LYS B CE  1 
ATOM   5206 N NZ  . LYS B 1 295 ? 12.352  41.387  8.385   1.00 40.63 ? 296 LYS B NZ  1 
ATOM   5207 N N   . PRO B 1 296 ? 5.793   42.272  9.515   1.00 25.69 ? 297 PRO B N   1 
ATOM   5208 C CA  . PRO B 1 296 ? 4.429   42.804  9.481   1.00 23.24 ? 297 PRO B CA  1 
ATOM   5209 C C   . PRO B 1 296 ? 4.083   43.255  8.074   1.00 23.28 ? 297 PRO B C   1 
ATOM   5210 O O   . PRO B 1 296 ? 4.933   43.776  7.344   1.00 23.88 ? 297 PRO B O   1 
ATOM   5211 C CB  . PRO B 1 296 ? 4.496   43.996  10.440  1.00 25.47 ? 297 PRO B CB  1 
ATOM   5212 C CG  . PRO B 1 296 ? 5.917   44.504  10.264  1.00 26.73 ? 297 PRO B CG  1 
ATOM   5213 C CD  . PRO B 1 296 ? 6.742   43.237  10.112  1.00 27.76 ? 297 PRO B CD  1 
ATOM   5214 N N   . ASN B 1 297 ? 2.807   43.103  7.715   1.00 22.84 ? 298 ASN B N   1 
ATOM   5215 C CA  . ASN B 1 297 ? 2.327   43.476  6.389   1.00 22.97 ? 298 ASN B CA  1 
ATOM   5216 C C   . ASN B 1 297 ? 0.965   44.132  6.504   1.00 22.77 ? 298 ASN B C   1 
ATOM   5217 O O   . ASN B 1 297 ? 0.071   43.597  7.165   1.00 22.35 ? 298 ASN B O   1 
ATOM   5218 C CB  . ASN B 1 297 ? 2.239   42.258  5.464   1.00 22.82 ? 298 ASN B CB  1 
ATOM   5219 C CG  . ASN B 1 297 ? 3.597   41.728  5.104   1.00 23.18 ? 298 ASN B CG  1 
ATOM   5220 O OD1 . ASN B 1 297 ? 4.270   42.285  4.244   1.00 23.78 ? 298 ASN B OD1 1 
ATOM   5221 N ND2 . ASN B 1 297 ? 4.026   40.662  5.779   1.00 25.37 ? 298 ASN B ND2 1 
ATOM   5222 N N   . LYS B 1 298 ? 0.817   45.299  5.872   1.00 23.15 ? 299 LYS B N   1 
ATOM   5223 C CA  . LYS B 1 298 ? -0.463  45.994  5.891   1.00 23.08 ? 299 LYS B CA  1 
ATOM   5224 C C   . LYS B 1 298 ? -1.524  45.177  5.160   1.00 22.90 ? 299 LYS B C   1 
ATOM   5225 O O   . LYS B 1 298 ? -1.265  44.586  4.105   1.00 24.04 ? 299 LYS B O   1 
ATOM   5226 C CB  . LYS B 1 298 ? -0.310  47.381  5.254   1.00 23.64 ? 299 LYS B CB  1 
ATOM   5227 C CG  . LYS B 1 298 ? -1.548  48.249  5.371   1.00 23.65 ? 299 LYS B CG  1 
ATOM   5228 C CD  . LYS B 1 298 ? -1.321  49.597  4.675   1.00 24.28 ? 299 LYS B CD  1 
ATOM   5229 C CE  . LYS B 1 298 ? -2.615  50.416  4.661   1.00 27.91 ? 299 LYS B CE  1 
ATOM   5230 N NZ  . LYS B 1 298 ? -2.520  51.608  3.780   1.00 30.20 ? 299 LYS B NZ  1 
ATOM   5231 N N   . VAL B 1 299 ? -2.723  45.105  5.738   1.00 22.65 ? 300 VAL B N   1 
ATOM   5232 C CA  . VAL B 1 299 ? -3.779  44.295  5.158   1.00 22.58 ? 300 VAL B CA  1 
ATOM   5233 C C   . VAL B 1 299 ? -4.713  45.178  4.344   1.00 23.03 ? 300 VAL B C   1 
ATOM   5234 O O   . VAL B 1 299 ? -4.806  46.399  4.530   1.00 23.28 ? 300 VAL B O   1 
ATOM   5235 C CB  . VAL B 1 299 ? -4.585  43.490  6.212   1.00 22.20 ? 300 VAL B CB  1 
ATOM   5236 C CG1 . VAL B 1 299 ? -3.656  42.724  7.133   1.00 21.86 ? 300 VAL B CG1 1 
ATOM   5237 C CG2 . VAL B 1 299 ? -5.495  44.412  7.024   1.00 22.31 ? 300 VAL B CG2 1 
ATOM   5238 N N   . THR B 1 300 ? -5.416  44.533  3.422   1.00 23.23 ? 301 THR B N   1 
ATOM   5239 C CA  . THR B 1 300 ? -6.438  45.154  2.598   1.00 23.79 ? 301 THR B CA  1 
ATOM   5240 C C   . THR B 1 300 ? -7.768  44.489  2.923   1.00 24.22 ? 301 THR B C   1 
ATOM   5241 O O   . THR B 1 300 ? -7.907  43.267  2.755   1.00 23.66 ? 301 THR B O   1 
ATOM   5242 C CB  . THR B 1 300 ? -6.087  44.985  1.121   1.00 27.20 ? 301 THR B CB  1 
ATOM   5243 O OG1 . THR B 1 300 ? -4.807  45.585  0.869   1.00 27.21 ? 301 THR B OG1 1 
ATOM   5244 C CG2 . THR B 1 300 ? -7.132  45.643  0.240   1.00 31.32 ? 301 THR B CG2 1 
ATOM   5245 N N   . ALA B 1 301 ? -8.731  45.279  3.398   1.00 23.98 ? 302 ALA B N   1 
ATOM   5246 C CA  . ALA B 1 301 ? -10.056 44.736  3.686   1.00 26.86 ? 302 ALA B CA  1 
ATOM   5247 C C   . ALA B 1 301 ? -10.688 44.162  2.418   1.00 28.10 ? 302 ALA B C   1 
ATOM   5248 O O   . ALA B 1 301 ? -10.511 44.696  1.321   1.00 26.30 ? 302 ALA B O   1 
ATOM   5249 C CB  . ALA B 1 301 ? -10.963 45.816  4.287   1.00 24.48 ? 302 ALA B CB  1 
ATOM   5250 N N   . ILE B 1 302 ? -11.439 43.076  2.573   1.00 27.62 ? 303 ILE B N   1 
ATOM   5251 C CA  . ILE B 1 302 ? -11.986 42.363  1.424   1.00 30.75 ? 303 ILE B CA  1 
ATOM   5252 C C   . ILE B 1 302 ? -13.248 43.064  0.950   1.00 37.87 ? 303 ILE B C   1 
ATOM   5253 O O   . ILE B 1 302 ? -14.104 43.447  1.755   1.00 41.73 ? 303 ILE B O   1 
ATOM   5254 C CB  . ILE B 1 302 ? -12.289 40.898  1.780   1.00 37.49 ? 303 ILE B CB  1 
ATOM   5255 C CG1 . ILE B 1 302 ? -13.033 40.875  3.113   1.00 36.23 ? 303 ILE B CG1 1 
ATOM   5256 C CG2 . ILE B 1 302 ? -11.022 40.030  1.796   1.00 30.87 ? 303 ILE B CG2 1 
ATOM   5257 C CD1 . ILE B 1 302 ? -13.217 39.552  3.653   1.00 39.83 ? 303 ILE B CD1 1 
ATOM   5258 N N   . SER B 1 303 ? -13.366 43.234  -0.366  1.00 39.02 ? 304 SER B N   1 
ATOM   5259 C CA  . SER B 1 303 ? -14.597 43.701  -0.989  1.00 48.13 ? 304 SER B CA  1 
ATOM   5260 C C   . SER B 1 303 ? -15.361 42.537  -1.613  1.00 55.89 ? 304 SER B C   1 
ATOM   5261 O O   . SER B 1 303 ? -16.467 42.204  -1.175  1.00 60.56 ? 304 SER B O   1 
ATOM   5262 C CB  . SER B 1 303 ? -14.282 44.782  -2.034  1.00 48.64 ? 304 SER B CB  1 
ATOM   5263 O OG  . SER B 1 303 ? -13.372 44.299  -3.006  1.00 51.85 ? 304 SER B OG  1 
ATOM   5264 N N   . LYS B 1 304 ? -14.763 41.884  -2.609  1.00 55.39 ? 305 LYS B N   1 
ATOM   5265 C CA  . LYS B 1 304 ? -15.317 40.688  -3.233  1.00 55.45 ? 305 LYS B CA  1 
ATOM   5266 C C   . LYS B 1 304 ? -14.402 39.507  -2.912  1.00 53.46 ? 305 LYS B C   1 
ATOM   5267 O O   . LYS B 1 304 ? -13.258 39.453  -3.381  1.00 49.05 ? 305 LYS B O   1 
ATOM   5268 C CB  . LYS B 1 304 ? -15.458 40.891  -4.742  1.00 60.47 ? 305 LYS B CB  1 
ATOM   5269 C CG  . LYS B 1 304 ? -16.345 39.864  -5.445  1.00 63.00 ? 305 LYS B CG  1 
ATOM   5270 C CD  . LYS B 1 304 ? -16.366 40.061  -6.963  1.00 65.39 ? 305 LYS B CD  1 
ATOM   5271 C CE  . LYS B 1 304 ? -15.051 39.624  -7.606  1.00 68.40 ? 305 LYS B CE  1 
ATOM   5272 N NZ  . LYS B 1 304 ? -14.731 38.179  -7.351  1.00 60.78 ? 305 LYS B NZ  1 
ATOM   5273 N N   . GLU B 1 305 ? -14.896 38.572  -2.108  1.00 49.86 ? 306 GLU B N   1 
ATOM   5274 C CA  . GLU B 1 305 ? -14.186 37.314  -1.940  1.00 48.25 ? 306 GLU B CA  1 
ATOM   5275 C C   . GLU B 1 305 ? -14.093 36.616  -3.298  1.00 43.33 ? 306 GLU B C   1 
ATOM   5276 O O   . GLU B 1 305 ? -15.038 36.686  -4.091  1.00 37.88 ? 306 GLU B O   1 
ATOM   5277 C CB  . GLU B 1 305 ? -14.896 36.418  -0.918  1.00 47.58 ? 306 GLU B CB  1 
ATOM   5278 C CG  . GLU B 1 305 ? -14.027 36.023  0.298   1.00 45.11 ? 306 GLU B CG  1 
ATOM   5279 C CD  . GLU B 1 305 ? -14.524 34.749  0.990   1.00 49.04 ? 306 GLU B CD  1 
ATOM   5280 O OE1 . GLU B 1 305 ? -13.804 33.723  0.958   1.00 51.19 ? 306 GLU B OE1 1 
ATOM   5281 O OE2 . GLU B 1 305 ? -15.654 34.766  1.537   1.00 54.75 ? 306 GLU B OE2 1 
ATOM   5282 N N   . PRO B 1 306 ? -12.973 35.963  -3.612  1.00 41.69 ? 307 PRO B N   1 
ATOM   5283 C CA  . PRO B 1 306 ? -12.846 35.324  -4.931  1.00 44.71 ? 307 PRO B CA  1 
ATOM   5284 C C   . PRO B 1 306 ? -13.949 34.299  -5.144  1.00 39.87 ? 307 PRO B C   1 
ATOM   5285 O O   . PRO B 1 306 ? -14.384 33.629  -4.204  1.00 37.59 ? 307 PRO B O   1 
ATOM   5286 C CB  . PRO B 1 306 ? -11.465 34.657  -4.883  1.00 37.77 ? 307 PRO B CB  1 
ATOM   5287 C CG  . PRO B 1 306 ? -10.784 35.222  -3.695  1.00 38.81 ? 307 PRO B CG  1 
ATOM   5288 C CD  . PRO B 1 306 ? -11.845 35.625  -2.728  1.00 40.46 ? 307 PRO B CD  1 
ATOM   5289 N N   . SER B 1 307 ? -14.413 34.200  -6.397  1.00 37.69 ? 308 SER B N   1 
ATOM   5290 C CA  . SER B 1 307 ? -15.533 33.319  -6.720  1.00 36.06 ? 308 SER B CA  1 
ATOM   5291 C C   . SER B 1 307 ? -15.138 31.850  -6.614  1.00 39.89 ? 308 SER B C   1 
ATOM   5292 O O   . SER B 1 307 ? -15.916 31.025  -6.117  1.00 36.67 ? 308 SER B O   1 
ATOM   5293 C CB  . SER B 1 307 ? -16.052 33.617  -8.130  1.00 42.32 ? 308 SER B CB  1 
ATOM   5294 O OG  . SER B 1 307 ? -16.562 34.934  -8.238  1.00 49.71 ? 308 SER B OG  1 
ATOM   5295 N N   . VAL B 1 308 ? -13.946 31.502  -7.094  1.00 36.00 ? 309 VAL B N   1 
ATOM   5296 C CA  . VAL B 1 308 ? -13.457 30.127  -7.102  1.00 30.44 ? 309 VAL B CA  1 
ATOM   5297 C C   . VAL B 1 308 ? -12.134 30.104  -6.344  1.00 30.52 ? 309 VAL B C   1 
ATOM   5298 O O   . VAL B 1 308 ? -11.219 30.875  -6.664  1.00 30.78 ? 309 VAL B O   1 
ATOM   5299 C CB  . VAL B 1 308 ? -13.287 29.599  -8.539  1.00 30.75 ? 309 VAL B CB  1 
ATOM   5300 C CG1 . VAL B 1 308 ? -12.906 28.113  -8.526  1.00 34.55 ? 309 VAL B CG1 1 
ATOM   5301 C CG2 . VAL B 1 308 ? -14.558 29.816  -9.340  1.00 39.51 ? 309 VAL B CG2 1 
ATOM   5302 N N   . LYS B 1 309 ? -12.034 29.228  -5.343  1.00 29.79 ? 310 LYS B N   1 
ATOM   5303 C CA  . LYS B 1 309 ? -11.001 29.327  -4.315  1.00 27.77 ? 310 LYS B CA  1 
ATOM   5304 C C   . LYS B 1 309 ? -10.248 28.013  -4.140  1.00 26.41 ? 310 LYS B C   1 
ATOM   5305 O O   . LYS B 1 309 ? -10.740 26.938  -4.482  1.00 27.68 ? 310 LYS B O   1 
ATOM   5306 C CB  . LYS B 1 309 ? -11.620 29.725  -2.964  1.00 29.99 ? 310 LYS B CB  1 
ATOM   5307 C CG  . LYS B 1 309 ? -12.358 31.047  -2.966  1.00 34.77 ? 310 LYS B CG  1 
ATOM   5308 C CD  . LYS B 1 309 ? -13.466 31.051  -1.918  1.00 34.96 ? 310 LYS B CD  1 
ATOM   5309 C CE  . LYS B 1 309 ? -14.766 30.527  -2.513  1.00 42.07 ? 310 LYS B CE  1 
ATOM   5310 N NZ  . LYS B 1 309 ? -15.720 30.051  -1.478  1.00 48.68 ? 310 LYS B NZ  1 
ATOM   5311 N N   . MET B 1 310 ? -9.034  28.109  -3.593  1.00 24.81 ? 311 MET B N   1 
ATOM   5312 C CA  . MET B 1 310 ? -8.325  26.952  -3.055  1.00 24.78 ? 311 MET B CA  1 
ATOM   5313 C C   . MET B 1 310 ? -7.630  27.395  -1.774  1.00 24.76 ? 311 MET B C   1 
ATOM   5314 O O   . MET B 1 310 ? -7.512  28.591  -1.497  1.00 22.06 ? 311 MET B O   1 
ATOM   5315 C CB  . MET B 1 310 ? -7.307  26.363  -4.050  1.00 25.95 ? 311 MET B CB  1 
ATOM   5316 C CG  . MET B 1 310 ? -6.180  27.333  -4.400  1.00 26.04 ? 311 MET B CG  1 
ATOM   5317 S SD  . MET B 1 310 ? -4.838  26.618  -5.367  1.00 31.70 ? 311 MET B SD  1 
ATOM   5318 C CE  . MET B 1 310 ? -4.125  25.531  -4.118  1.00 27.65 ? 311 MET B CE  1 
ATOM   5319 N N   . TYR B 1 311 ? -7.161  26.416  -0.994  1.00 22.31 ? 312 TYR B N   1 
ATOM   5320 C CA  . TYR B 1 311 ? -6.666  26.652  0.357   1.00 24.10 ? 312 TYR B CA  1 
ATOM   5321 C C   . TYR B 1 311 ? -5.427  25.809  0.623   1.00 19.83 ? 312 TYR B C   1 
ATOM   5322 O O   . TYR B 1 311 ? -5.332  24.670  0.156   1.00 20.59 ? 312 TYR B O   1 
ATOM   5323 C CB  . TYR B 1 311 ? -7.725  26.304  1.402   1.00 21.93 ? 312 TYR B CB  1 
ATOM   5324 C CG  . TYR B 1 311 ? -9.038  27.031  1.201   1.00 22.20 ? 312 TYR B CG  1 
ATOM   5325 C CD1 . TYR B 1 311 ? -10.015 26.530  0.345   1.00 25.71 ? 312 TYR B CD1 1 
ATOM   5326 C CD2 . TYR B 1 311 ? -9.303  28.217  1.881   1.00 24.73 ? 312 TYR B CD2 1 
ATOM   5327 C CE1 . TYR B 1 311 ? -11.218 27.203  0.167   1.00 25.90 ? 312 TYR B CE1 1 
ATOM   5328 C CE2 . TYR B 1 311 ? -10.508 28.905  1.712   1.00 26.11 ? 312 TYR B CE2 1 
ATOM   5329 C CZ  . TYR B 1 311 ? -11.454 28.397  0.851   1.00 28.78 ? 312 TYR B CZ  1 
ATOM   5330 O OH  . TYR B 1 311 ? -12.640 29.077  0.692   1.00 28.42 ? 312 TYR B OH  1 
ATOM   5331 N N   . HIS B 1 312 ? -4.493  26.350  1.415   1.00 19.39 ? 313 HIS B N   1 
ATOM   5332 C CA  . HIS B 1 312 ? -3.351  25.537  1.832   1.00 18.09 ? 313 HIS B CA  1 
ATOM   5333 C C   . HIS B 1 312 ? -2.818  25.997  3.185   1.00 19.21 ? 313 HIS B C   1 
ATOM   5334 O O   . HIS B 1 312 ? -3.176  27.068  3.698   1.00 18.08 ? 313 HIS B O   1 
ATOM   5335 C CB  . HIS B 1 312 ? -2.246  25.498  0.733   1.00 22.07 ? 313 HIS B CB  1 
ATOM   5336 C CG  . HIS B 1 312 ? -1.277  26.655  0.711   1.00 21.12 ? 313 HIS B CG  1 
ATOM   5337 N ND1 . HIS B 1 312 ? -0.310  26.761  -0.268  1.00 23.32 ? 313 HIS B ND1 1 
ATOM   5338 C CD2 . HIS B 1 312 ? -1.099  27.728  1.531   1.00 19.77 ? 313 HIS B CD2 1 
ATOM   5339 C CE1 . HIS B 1 312 ? 0.406   27.853  -0.058  1.00 22.33 ? 313 HIS B CE1 1 
ATOM   5340 N NE2 . HIS B 1 312 ? -0.042  28.450  1.034   1.00 22.76 ? 313 HIS B NE2 1 
ATOM   5341 N N   . LYS B 1 313 ? -1.971  25.147  3.772   1.00 18.95 ? 314 LYS B N   1 
ATOM   5342 C CA  . LYS B 1 313 ? -1.285  25.460  5.023   1.00 20.52 ? 314 LYS B CA  1 
ATOM   5343 C C   . LYS B 1 313 ? -0.025  24.602  5.153   1.00 18.77 ? 314 LYS B C   1 
ATOM   5344 O O   . LYS B 1 313 ? -0.051  23.389  4.875   1.00 17.97 ? 314 LYS B O   1 
ATOM   5345 C CB  . LYS B 1 313 ? -2.223  25.242  6.226   1.00 18.71 ? 314 LYS B CB  1 
ATOM   5346 C CG  . LYS B 1 313 ? -1.647  25.679  7.582   1.00 20.14 ? 314 LYS B CG  1 
ATOM   5347 C CD  . LYS B 1 313 ? -1.628  27.198  7.724   1.00 20.94 ? 314 LYS B CD  1 
ATOM   5348 C CE  . LYS B 1 313 ? -0.837  27.648  8.957   1.00 24.31 ? 314 LYS B CE  1 
ATOM   5349 N NZ  . LYS B 1 313 ? 0.603   27.892  8.636   1.00 27.34 ? 314 LYS B NZ  1 
ATOM   5350 N N   . THR B 1 314 ? 1.068   25.223  5.609   1.00 20.41 ? 315 THR B N   1 
ATOM   5351 C CA  . THR B 1 314 ? 2.291   24.508  5.957   1.00 20.46 ? 315 THR B CA  1 
ATOM   5352 C C   . THR B 1 314 ? 2.470   24.442  7.471   1.00 22.62 ? 315 THR B C   1 
ATOM   5353 O O   . THR B 1 314 ? 1.963   25.286  8.218   1.00 23.82 ? 315 THR B O   1 
ATOM   5354 C CB  . THR B 1 314 ? 3.539   25.171  5.344   1.00 21.10 ? 315 THR B CB  1 
ATOM   5355 O OG1 . THR B 1 314 ? 3.557   26.564  5.673   1.00 23.81 ? 315 THR B OG1 1 
ATOM   5356 C CG2 . THR B 1 314 ? 3.545   25.051  3.834   1.00 22.86 ? 315 THR B CG2 1 
ATOM   5357 N N   . GLY B 1 315 ? 3.231   23.443  7.910   1.00 21.46 ? 316 GLY B N   1 
ATOM   5358 C CA  . GLY B 1 315 ? 3.615   23.330  9.311   1.00 21.42 ? 316 GLY B CA  1 
ATOM   5359 C C   . GLY B 1 315 ? 4.982   22.694  9.436   1.00 21.60 ? 316 GLY B C   1 
ATOM   5360 O O   . GLY B 1 315 ? 5.347   21.811  8.650   1.00 21.73 ? 316 GLY B O   1 
ATOM   5361 N N   . THR B 1 316 ? 5.726   23.109  10.462  1.00 24.90 ? 317 THR B N   1 
ATOM   5362 C CA  . THR B 1 316 ? 7.089   22.626  10.669  1.00 24.72 ? 317 THR B CA  1 
ATOM   5363 C C   . THR B 1 316 ? 7.382   22.499  12.164  1.00 26.40 ? 317 THR B C   1 
ATOM   5364 O O   . THR B 1 316 ? 6.991   23.370  12.940  1.00 24.85 ? 317 THR B O   1 
ATOM   5365 C CB  . THR B 1 316 ? 8.107   23.581  10.008  1.00 26.62 ? 317 THR B CB  1 
ATOM   5366 O OG1 . THR B 1 316 ? 7.863   23.677  8.596   1.00 27.38 ? 317 THR B OG1 1 
ATOM   5367 C CG2 . THR B 1 316 ? 9.529   23.098  10.231  1.00 31.55 ? 317 THR B CG2 1 
ATOM   5368 N N   . THR B 1 317 ? 8.047   21.405  12.576  1.00 26.06 ? 318 THR B N   1 
ATOM   5369 C CA  . THR B 1 317 ? 8.620   21.306  13.928  1.00 28.74 ? 318 THR B CA  1 
ATOM   5370 C C   . THR B 1 317 ? 10.048  20.772  13.856  1.00 28.25 ? 318 THR B C   1 
ATOM   5371 O O   . THR B 1 317 ? 10.586  20.490  12.779  1.00 25.39 ? 318 THR B O   1 
ATOM   5372 C CB  . THR B 1 317 ? 7.805   20.406  14.878  1.00 29.06 ? 318 THR B CB  1 
ATOM   5373 O OG1 . THR B 1 317 ? 7.964   19.014  14.525  1.00 27.91 ? 318 THR B OG1 1 
ATOM   5374 C CG2 . THR B 1 317 ? 6.326   20.795  14.884  1.00 26.24 ? 318 THR B CG2 1 
ATOM   5375 N N   . ASN B 1 318 ? 10.654  20.609  15.037  1.00 28.00 ? 319 ASN B N   1 
ATOM   5376 C CA  . ASN B 1 318 ? 11.997  20.059  15.138  1.00 31.04 ? 319 ASN B CA  1 
ATOM   5377 C C   . ASN B 1 318 ? 12.079  18.614  14.659  1.00 32.15 ? 319 ASN B C   1 
ATOM   5378 O O   . ASN B 1 318 ? 13.189  18.087  14.535  1.00 33.14 ? 319 ASN B O   1 
ATOM   5379 C CB  . ASN B 1 318 ? 12.501  20.150  16.583  1.00 37.12 ? 319 ASN B CB  1 
ATOM   5380 C CG  . ASN B 1 318 ? 12.943  21.560  16.958  1.00 43.69 ? 319 ASN B CG  1 
ATOM   5381 O OD1 . ASN B 1 318 ? 13.389  22.339  16.101  1.00 40.37 ? 319 ASN B OD1 1 
ATOM   5382 N ND2 . ASN B 1 318 ? 12.817  21.899  18.241  1.00 44.33 ? 319 ASN B ND2 1 
ATOM   5383 N N   . ARG B 1 319 ? 10.945  17.968  14.384  1.00 29.97 ? 320 ARG B N   1 
ATOM   5384 C CA  . ARG B 1 319 ? 10.976  16.625  13.817  1.00 28.62 ? 320 ARG B CA  1 
ATOM   5385 C C   . ARG B 1 319 ? 9.765   16.386  12.920  1.00 27.21 ? 320 ARG B C   1 
ATOM   5386 O O   . ARG B 1 319 ? 9.199   15.284  12.894  1.00 26.34 ? 320 ARG B O   1 
ATOM   5387 C CB  . ARG B 1 319 ? 11.077  15.557  14.912  1.00 35.17 ? 320 ARG B CB  1 
ATOM   5388 C CG  . ARG B 1 319 ? 10.038  15.650  16.016  1.00 35.74 ? 320 ARG B CG  1 
ATOM   5389 C CD  . ARG B 1 319 ? 10.523  14.891  17.265  1.00 39.11 ? 320 ARG B CD  1 
ATOM   5390 N NE  . ARG B 1 319 ? 9.563   15.001  18.355  1.00 41.96 ? 320 ARG B NE  1 
ATOM   5391 C CZ  . ARG B 1 319 ? 9.788   14.626  19.607  1.00 43.18 ? 320 ARG B CZ  1 
ATOM   5392 N NH1 . ARG B 1 319 ? 10.950  14.116  19.978  1.00 42.15 ? 320 ARG B NH1 1 
ATOM   5393 N NH2 . ARG B 1 319 ? 8.822   14.775  20.510  1.00 45.03 ? 320 ARG B NH2 1 
ATOM   5394 N N   . SER B 1 320 ? 9.390   17.392  12.127  1.00 23.18 ? 321 SER B N   1 
ATOM   5395 C CA  . SER B 1 320 ? 8.306   17.175  11.176  1.00 23.19 ? 321 SER B CA  1 
ATOM   5396 C C   . SER B 1 320 ? 8.250   18.300  10.152  1.00 24.64 ? 321 SER B C   1 
ATOM   5397 O O   . SER B 1 320 ? 8.673   19.432  10.413  1.00 25.35 ? 321 SER B O   1 
ATOM   5398 C CB  . SER B 1 320 ? 6.943   17.088  11.874  1.00 25.29 ? 321 SER B CB  1 
ATOM   5399 O OG  . SER B 1 320 ? 6.610   18.346  12.430  1.00 26.96 ? 321 SER B OG  1 
ATOM   5400 N N   . GLY B 1 321 ? 7.719   17.958  8.993   1.00 22.92 ? 322 GLY B N   1 
ATOM   5401 C CA  . GLY B 1 321 ? 7.266   18.947  8.031   1.00 23.27 ? 322 GLY B CA  1 
ATOM   5402 C C   . GLY B 1 321 ? 5.912   18.491  7.529   1.00 22.68 ? 322 GLY B C   1 
ATOM   5403 O O   . GLY B 1 321 ? 5.668   17.292  7.381   1.00 21.77 ? 322 GLY B O   1 
ATOM   5404 N N   . THR B 1 322 ? 5.022   19.458  7.298   1.00 19.81 ? 323 THR B N   1 
ATOM   5405 C CA  . THR B 1 322 ? 3.631   19.179  6.941   1.00 19.10 ? 323 THR B CA  1 
ATOM   5406 C C   . THR B 1 322 ? 3.166   20.130  5.848   1.00 19.09 ? 323 THR B C   1 
ATOM   5407 O O   . THR B 1 322 ? 3.558   21.306  5.830   1.00 19.08 ? 323 THR B O   1 
ATOM   5408 C CB  . THR B 1 322 ? 2.695   19.307  8.157   1.00 20.67 ? 323 THR B CB  1 
ATOM   5409 O OG1 . THR B 1 322 ? 3.202   18.537  9.255   1.00 28.07 ? 323 THR B OG1 1 
ATOM   5410 C CG2 . THR B 1 322 ? 1.283   18.796  7.826   1.00 19.14 ? 323 THR B CG2 1 
ATOM   5411 N N   . TYR B 1 323 ? 2.342   19.617  4.925   1.00 17.83 ? 324 TYR B N   1 
ATOM   5412 C CA  . TYR B 1 323 ? 1.665   20.475  3.953   1.00 18.48 ? 324 TYR B CA  1 
ATOM   5413 C C   . TYR B 1 323 ? 0.295   19.895  3.640   1.00 19.70 ? 324 TYR B C   1 
ATOM   5414 O O   . TYR B 1 323 ? 0.171   18.684  3.403   1.00 19.35 ? 324 TYR B O   1 
ATOM   5415 C CB  . TYR B 1 323 ? 2.471   20.611  2.655   1.00 17.91 ? 324 TYR B CB  1 
ATOM   5416 C CG  . TYR B 1 323 ? 1.881   21.580  1.635   1.00 17.76 ? 324 TYR B CG  1 
ATOM   5417 C CD1 . TYR B 1 323 ? 1.671   22.923  1.948   1.00 19.57 ? 324 TYR B CD1 1 
ATOM   5418 C CD2 . TYR B 1 323 ? 1.572   21.160  0.351   1.00 19.12 ? 324 TYR B CD2 1 
ATOM   5419 C CE1 . TYR B 1 323 ? 1.147   23.820  1.000   1.00 19.20 ? 324 TYR B CE1 1 
ATOM   5420 C CE2 . TYR B 1 323 ? 1.052   22.045  -0.612  1.00 20.04 ? 324 TYR B CE2 1 
ATOM   5421 C CZ  . TYR B 1 323 ? 0.841   23.369  -0.279  1.00 19.45 ? 324 TYR B CZ  1 
ATOM   5422 O OH  . TYR B 1 323 ? 0.333   24.231  -1.232  1.00 21.36 ? 324 TYR B OH  1 
ATOM   5423 N N   . VAL B 1 324 ? -0.723  20.753  3.614   1.00 18.78 ? 325 VAL B N   1 
ATOM   5424 C CA  . VAL B 1 324 ? -2.069  20.341  3.231   1.00 19.30 ? 325 VAL B CA  1 
ATOM   5425 C C   . VAL B 1 324 ? -2.654  21.354  2.255   1.00 17.45 ? 325 VAL B C   1 
ATOM   5426 O O   . VAL B 1 324 ? -2.450  22.569  2.404   1.00 18.12 ? 325 VAL B O   1 
ATOM   5427 C CB  . VAL B 1 324 ? -2.994  20.147  4.455   1.00 19.62 ? 325 VAL B CB  1 
ATOM   5428 C CG1 . VAL B 1 324 ? -2.538  18.923  5.283   1.00 20.48 ? 325 VAL B CG1 1 
ATOM   5429 C CG2 . VAL B 1 324 ? -3.068  21.379  5.321   1.00 20.07 ? 325 VAL B CG2 1 
ATOM   5430 N N   . VAL B 1 325 ? -3.396  20.853  1.260   1.00 19.31 ? 326 VAL B N   1 
ATOM   5431 C CA  . VAL B 1 325 ? -3.969  21.717  0.221   1.00 19.24 ? 326 VAL B CA  1 
ATOM   5432 C C   . VAL B 1 325 ? -5.251  21.071  -0.310  1.00 21.40 ? 326 VAL B C   1 
ATOM   5433 O O   . VAL B 1 325 ? -5.330  19.841  -0.450  1.00 22.50 ? 326 VAL B O   1 
ATOM   5434 C CB  . VAL B 1 325 ? -2.937  21.959  -0.907  1.00 18.82 ? 326 VAL B CB  1 
ATOM   5435 C CG1 . VAL B 1 325 ? -2.472  20.629  -1.516  1.00 19.56 ? 326 VAL B CG1 1 
ATOM   5436 C CG2 . VAL B 1 325 ? -3.507  22.828  -1.998  1.00 19.11 ? 326 VAL B CG2 1 
ATOM   5437 N N   . PHE B 1 326 ? -6.262  21.890  -0.610  1.00 19.57 ? 327 PHE B N   1 
ATOM   5438 C CA  . PHE B 1 326 ? -7.455  21.345  -1.257  1.00 22.95 ? 327 PHE B CA  1 
ATOM   5439 C C   . PHE B 1 326 ? -8.103  22.370  -2.188  1.00 22.92 ? 327 PHE B C   1 
ATOM   5440 O O   . PHE B 1 326 ? -7.970  23.587  -2.009  1.00 21.61 ? 327 PHE B O   1 
ATOM   5441 C CB  . PHE B 1 326 ? -8.488  20.812  -0.234  1.00 22.56 ? 327 PHE B CB  1 
ATOM   5442 C CG  . PHE B 1 326 ? -9.211  21.879  0.568   1.00 24.81 ? 327 PHE B CG  1 
ATOM   5443 C CD1 . PHE B 1 326 ? -8.641  22.418  1.709   1.00 21.22 ? 327 PHE B CD1 1 
ATOM   5444 C CD2 . PHE B 1 326 ? -10.504 22.284  0.217   1.00 22.57 ? 327 PHE B CD2 1 
ATOM   5445 C CE1 . PHE B 1 326 ? -9.317  23.382  2.463   1.00 20.46 ? 327 PHE B CE1 1 
ATOM   5446 C CE2 . PHE B 1 326 ? -11.184 23.241  0.967   1.00 24.64 ? 327 PHE B CE2 1 
ATOM   5447 C CZ  . PHE B 1 326 ? -10.592 23.784  2.104   1.00 23.43 ? 327 PHE B CZ  1 
ATOM   5448 N N   . ILE B 1 327 ? -8.811  21.850  -3.192  1.00 21.25 ? 328 ILE B N   1 
ATOM   5449 C CA  . ILE B 1 327 ? -9.448  22.661  -4.226  1.00 27.00 ? 328 ILE B CA  1 
ATOM   5450 C C   . ILE B 1 327 ? -10.895 22.209  -4.403  1.00 28.95 ? 328 ILE B C   1 
ATOM   5451 O O   . ILE B 1 327 ? -11.147 21.178  -5.050  1.00 29.20 ? 328 ILE B O   1 
ATOM   5452 C CB  . ILE B 1 327 ? -8.685  22.565  -5.555  1.00 29.08 ? 328 ILE B CB  1 
ATOM   5453 C CG1 . ILE B 1 327 ? -7.191  22.832  -5.336  1.00 27.39 ? 328 ILE B CG1 1 
ATOM   5454 C CG2 . ILE B 1 327 ? -9.301  23.509  -6.582  1.00 28.30 ? 328 ILE B CG2 1 
ATOM   5455 C CD1 . ILE B 1 327 ? -6.316  22.304  -6.439  1.00 31.73 ? 328 ILE B CD1 1 
ATOM   5456 N N   . PRO B 1 328 ? -11.872 22.939  -3.852  1.00 27.97 ? 329 PRO B N   1 
ATOM   5457 C CA  . PRO B 1 328 ? -13.265 22.451  -3.899  1.00 30.49 ? 329 PRO B CA  1 
ATOM   5458 C C   . PRO B 1 328 ? -13.792 22.188  -5.299  1.00 32.33 ? 329 PRO B C   1 
ATOM   5459 O O   . PRO B 1 328 ? -14.437 21.154  -5.523  1.00 32.26 ? 329 PRO B O   1 
ATOM   5460 C CB  . PRO B 1 328 ? -14.041 23.574  -3.203  1.00 29.98 ? 329 PRO B CB  1 
ATOM   5461 C CG  . PRO B 1 328 ? -13.034 24.171  -2.245  1.00 28.84 ? 329 PRO B CG  1 
ATOM   5462 C CD  . PRO B 1 328 ? -11.730 24.139  -3.005  1.00 26.27 ? 329 PRO B CD  1 
ATOM   5463 N N   . LYS B 1 329 ? -13.523 23.082  -6.253  1.00 29.44 ? 330 LYS B N   1 
ATOM   5464 C CA  . LYS B 1 329 ? -14.075 22.918  -7.600  1.00 35.91 ? 330 LYS B CA  1 
ATOM   5465 C C   . LYS B 1 329 ? -13.629 21.606  -8.234  1.00 36.64 ? 330 LYS B C   1 
ATOM   5466 O O   . LYS B 1 329 ? -14.377 21.006  -9.017  1.00 36.93 ? 330 LYS B O   1 
ATOM   5467 C CB  . LYS B 1 329 ? -13.667 24.098  -8.486  1.00 33.67 ? 330 LYS B CB  1 
ATOM   5468 C CG  . LYS B 1 329 ? -14.059 23.966  -9.958  1.00 43.21 ? 330 LYS B CG  1 
ATOM   5469 C CD  . LYS B 1 329 ? -13.251 24.928  -10.827 1.00 42.19 ? 330 LYS B CD  1 
ATOM   5470 C CE  . LYS B 1 329 ? -13.471 24.679  -12.304 1.00 42.73 ? 330 LYS B CE  1 
ATOM   5471 N NZ  . LYS B 1 329 ? -14.886 24.916  -12.663 1.00 49.90 ? 330 LYS B NZ  1 
ATOM   5472 N N   . GLU B 1 330 ? -12.427 21.142  -7.904  1.00 31.40 ? 331 GLU B N   1 
ATOM   5473 C CA  . GLU B 1 330 ? -11.867 19.933  -8.490  1.00 33.12 ? 331 GLU B CA  1 
ATOM   5474 C C   . GLU B 1 330 ? -12.066 18.702  -7.616  1.00 30.93 ? 331 GLU B C   1 
ATOM   5475 O O   . GLU B 1 330 ? -11.659 17.603  -8.015  1.00 34.37 ? 331 GLU B O   1 
ATOM   5476 C CB  . GLU B 1 330 ? -10.376 20.142  -8.779  1.00 34.60 ? 331 GLU B CB  1 
ATOM   5477 C CG  . GLU B 1 330 ? -10.091 21.331  -9.689  1.00 38.40 ? 331 GLU B CG  1 
ATOM   5478 C CD  . GLU B 1 330 ? -10.603 21.120  -11.100 1.00 45.26 ? 331 GLU B CD  1 
ATOM   5479 O OE1 . GLU B 1 330 ? -11.725 21.578  -11.408 1.00 47.77 ? 331 GLU B OE1 1 
ATOM   5480 O OE2 . GLU B 1 330 ? -9.888  20.486  -11.905 1.00 49.40 ? 331 GLU B OE2 1 
ATOM   5481 N N   . ASN B 1 331 ? -12.685 18.859  -6.445  1.00 29.25 ? 332 ASN B N   1 
ATOM   5482 C CA  . ASN B 1 331 ? -12.983 17.753  -5.535  1.00 30.75 ? 332 ASN B CA  1 
ATOM   5483 C C   . ASN B 1 331 ? -11.728 16.943  -5.217  1.00 29.88 ? 332 ASN B C   1 
ATOM   5484 O O   . ASN B 1 331 ? -11.736 15.708  -5.233  1.00 29.39 ? 332 ASN B O   1 
ATOM   5485 C CB  . ASN B 1 331 ? -14.073 16.848  -6.111  1.00 35.11 ? 332 ASN B CB  1 
ATOM   5486 C CG  . ASN B 1 331 ? -15.351 17.593  -6.401  1.00 36.58 ? 332 ASN B CG  1 
ATOM   5487 O OD1 . ASN B 1 331 ? -15.848 17.585  -7.528  1.00 44.66 ? 332 ASN B OD1 1 
ATOM   5488 N ND2 . ASN B 1 331 ? -15.904 18.231  -5.380  1.00 44.19 ? 332 ASN B ND2 1 
ATOM   5489 N N   . ILE B 1 332 ? -10.638 17.650  -4.911  1.00 29.86 ? 333 ILE B N   1 
ATOM   5490 C CA  . ILE B 1 332 ? -9.340  17.003  -4.730  1.00 25.71 ? 333 ILE B CA  1 
ATOM   5491 C C   . ILE B 1 332 ? -8.562  17.726  -3.638  1.00 26.27 ? 333 ILE B C   1 
ATOM   5492 O O   . ILE B 1 332 ? -8.750  18.924  -3.400  1.00 25.35 ? 333 ILE B O   1 
ATOM   5493 C CB  . ILE B 1 332 ? -8.555  16.965  -6.066  1.00 29.66 ? 333 ILE B CB  1 
ATOM   5494 C CG1 . ILE B 1 332 ? -7.410  15.953  -5.999  1.00 32.44 ? 333 ILE B CG1 1 
ATOM   5495 C CG2 . ILE B 1 332 ? -8.051  18.361  -6.442  1.00 28.68 ? 333 ILE B CG2 1 
ATOM   5496 C CD1 . ILE B 1 332 ? -6.869  15.534  -7.374  1.00 33.10 ? 333 ILE B CD1 1 
ATOM   5497 N N   . GLY B 1 333 ? -7.680  16.980  -2.969  1.00 22.08 ? 334 GLY B N   1 
ATOM   5498 C CA  . GLY B 1 333 ? -6.796  17.536  -1.958  1.00 20.55 ? 334 GLY B CA  1 
ATOM   5499 C C   . GLY B 1 333 ? -5.592  16.640  -1.776  1.00 23.31 ? 334 GLY B C   1 
ATOM   5500 O O   . GLY B 1 333 ? -5.560  15.501  -2.252  1.00 21.77 ? 334 GLY B O   1 
ATOM   5501 N N   . LEU B 1 334 ? -4.601  17.156  -1.049  1.00 19.46 ? 335 LEU B N   1 
ATOM   5502 C CA  . LEU B 1 334 ? -3.359  16.419  -0.840  1.00 21.22 ? 335 LEU B CA  1 
ATOM   5503 C C   . LEU B 1 334 ? -2.797  16.732  0.539   1.00 20.15 ? 335 LEU B C   1 
ATOM   5504 O O   . LEU B 1 334 ? -2.909  17.867  1.015   1.00 19.36 ? 335 LEU B O   1 
ATOM   5505 C CB  . LEU B 1 334 ? -2.311  16.752  -1.914  1.00 22.68 ? 335 LEU B CB  1 
ATOM   5506 C CG  . LEU B 1 334 ? -0.949  16.030  -1.880  1.00 18.71 ? 335 LEU B CG  1 
ATOM   5507 C CD1 . LEU B 1 334 ? -0.387  15.904  -3.280  1.00 21.88 ? 335 LEU B CD1 1 
ATOM   5508 C CD2 . LEU B 1 334 ? 0.087   16.698  -0.957  1.00 20.68 ? 335 LEU B CD2 1 
ATOM   5509 N N   . VAL B 1 335 ? -2.189  15.717  1.163   1.00 20.82 ? 336 VAL B N   1 
ATOM   5510 C CA  . VAL B 1 335 ? -1.508  15.836  2.452   1.00 19.48 ? 336 VAL B CA  1 
ATOM   5511 C C   . VAL B 1 335 ? -0.115  15.223  2.331   1.00 17.78 ? 336 VAL B C   1 
ATOM   5512 O O   . VAL B 1 335 ? 0.022   14.075  1.877   1.00 21.03 ? 336 VAL B O   1 
ATOM   5513 C CB  . VAL B 1 335 ? -2.297  15.122  3.569   1.00 21.74 ? 336 VAL B CB  1 
ATOM   5514 C CG1 . VAL B 1 335 ? -1.542  15.173  4.896   1.00 19.91 ? 336 VAL B CG1 1 
ATOM   5515 C CG2 . VAL B 1 335 ? -3.690  15.714  3.709   1.00 21.61 ? 336 VAL B CG2 1 
ATOM   5516 N N   . MET B 1 336 ? 0.905   15.954  2.784   1.00 18.64 ? 337 MET B N   1 
ATOM   5517 C CA  . MET B 1 336 ? 2.253   15.407  2.968   1.00 17.55 ? 337 MET B CA  1 
ATOM   5518 C C   . MET B 1 336 ? 2.637   15.514  4.435   1.00 17.52 ? 337 MET B C   1 
ATOM   5519 O O   . MET B 1 336 ? 2.566   16.598  5.020   1.00 17.43 ? 337 MET B O   1 
ATOM   5520 C CB  . MET B 1 336 ? 3.292   16.130  2.099   1.00 19.01 ? 337 MET B CB  1 
ATOM   5521 C CG  . MET B 1 336 ? 4.759   15.698  2.351   1.00 22.00 ? 337 MET B CG  1 
ATOM   5522 S SD  . MET B 1 336 ? 5.974   17.024  2.103   1.00 26.62 ? 337 MET B SD  1 
ATOM   5523 C CE  . MET B 1 336 ? 5.894   17.841  3.702   1.00 21.63 ? 337 MET B CE  1 
ATOM   5524 N N   . LEU B 1 337 ? 3.014   14.387  5.035   1.00 20.30 ? 338 LEU B N   1 
ATOM   5525 C CA  . LEU B 1 337 ? 3.571   14.345  6.383   1.00 18.93 ? 338 LEU B CA  1 
ATOM   5526 C C   . LEU B 1 337 ? 4.988   13.788  6.312   1.00 19.44 ? 338 LEU B C   1 
ATOM   5527 O O   . LEU B 1 337 ? 5.215   12.731  5.710   1.00 22.84 ? 338 LEU B O   1 
ATOM   5528 C CB  . LEU B 1 337 ? 2.710   13.473  7.321   1.00 17.93 ? 338 LEU B CB  1 
ATOM   5529 C CG  . LEU B 1 337 ? 1.182   13.674  7.315   1.00 17.56 ? 338 LEU B CG  1 
ATOM   5530 C CD1 . LEU B 1 337 ? 0.456   12.649  8.207   1.00 19.96 ? 338 LEU B CD1 1 
ATOM   5531 C CD2 . LEU B 1 337 ? 0.808   15.114  7.722   1.00 19.81 ? 338 LEU B CD2 1 
ATOM   5532 N N   . THR B 1 338 ? 5.933   14.474  6.935   1.00 21.82 ? 339 THR B N   1 
ATOM   5533 C CA  . THR B 1 338 ? 7.297   13.975  7.037   1.00 22.58 ? 339 THR B CA  1 
ATOM   5534 C C   . THR B 1 338 ? 7.733   14.069  8.488   1.00 25.08 ? 339 THR B C   1 
ATOM   5535 O O   . THR B 1 338 ? 7.138   14.795  9.287   1.00 24.66 ? 339 THR B O   1 
ATOM   5536 C CB  . THR B 1 338 ? 8.293   14.762  6.156   1.00 23.36 ? 339 THR B CB  1 
ATOM   5537 O OG1 . THR B 1 338 ? 8.373   16.117  6.627   1.00 29.29 ? 339 THR B OG1 1 
ATOM   5538 C CG2 . THR B 1 338 ? 7.850   14.781  4.683   1.00 24.44 ? 339 THR B CG2 1 
ATOM   5539 N N   . ASN B 1 339 ? 8.786   13.324  8.818   1.00 24.43 ? 340 ASN B N   1 
ATOM   5540 C CA  . ASN B 1 339 ? 9.406   13.391  10.132  1.00 22.67 ? 340 ASN B CA  1 
ATOM   5541 C C   . ASN B 1 339 ? 10.724  14.148  10.083  1.00 23.61 ? 340 ASN B C   1 
ATOM   5542 O O   . ASN B 1 339 ? 11.583  13.952  10.943  1.00 24.83 ? 340 ASN B O   1 
ATOM   5543 C CB  . ASN B 1 339 ? 9.586   11.982  10.729  1.00 23.20 ? 340 ASN B CB  1 
ATOM   5544 C CG  . ASN B 1 339 ? 10.364  11.024  9.824   1.00 22.87 ? 340 ASN B CG  1 
ATOM   5545 O OD1 . ASN B 1 339 ? 11.009  11.418  8.852   1.00 23.94 ? 340 ASN B OD1 1 
ATOM   5546 N ND2 . ASN B 1 339 ? 10.310  9.738   10.168  1.00 23.34 ? 340 ASN B ND2 1 
ATOM   5547 N N   . LYS B 1 340 ? 10.883  15.029  9.093   1.00 23.20 ? 341 LYS B N   1 
ATOM   5548 C CA  . LYS B 1 340 ? 12.007  15.948  9.003   1.00 25.57 ? 341 LYS B CA  1 
ATOM   5549 C C   . LYS B 1 340 ? 11.573  17.155  8.183   1.00 23.80 ? 341 LYS B C   1 
ATOM   5550 O O   . LYS B 1 340 ? 10.934  17.006  7.138   1.00 24.03 ? 341 LYS B O   1 
ATOM   5551 C CB  . LYS B 1 340 ? 13.233  15.314  8.348   1.00 25.99 ? 341 LYS B CB  1 
ATOM   5552 C CG  . LYS B 1 340 ? 14.493  16.182  8.482   1.00 28.76 ? 341 LYS B CG  1 
ATOM   5553 C CD  . LYS B 1 340 ? 15.371  16.108  7.255   1.00 29.82 ? 341 LYS B CD  1 
ATOM   5554 C CE  . LYS B 1 340 ? 16.744  16.718  7.533   1.00 30.54 ? 341 LYS B CE  1 
ATOM   5555 N NZ  . LYS B 1 340 ? 17.400  17.110  6.261   1.00 29.17 ? 341 LYS B NZ  1 
ATOM   5556 N N   . ARG B 1 341 ? 11.923  18.345  8.660   1.00 24.56 ? 342 ARG B N   1 
ATOM   5557 C CA  . ARG B 1 341 ? 11.641  19.558  7.905   1.00 24.82 ? 342 ARG B CA  1 
ATOM   5558 C C   . ARG B 1 341 ? 12.340  19.535  6.544   1.00 28.66 ? 342 ARG B C   1 
ATOM   5559 O O   . ARG B 1 341 ? 13.508  19.144  6.433   1.00 28.58 ? 342 ARG B O   1 
ATOM   5560 C CB  . ARG B 1 341 ? 12.093  20.769  8.733   1.00 28.72 ? 342 ARG B CB  1 
ATOM   5561 C CG  . ARG B 1 341 ? 12.584  21.948  7.941   1.00 40.06 ? 342 ARG B CG  1 
ATOM   5562 C CD  . ARG B 1 341 ? 13.632  22.729  8.743   1.00 44.44 ? 342 ARG B CD  1 
ATOM   5563 N NE  . ARG B 1 341 ? 13.036  23.575  9.773   1.00 48.87 ? 342 ARG B NE  1 
ATOM   5564 C CZ  . ARG B 1 341 ? 12.927  24.896  9.685   1.00 53.82 ? 342 ARG B CZ  1 
ATOM   5565 N NH1 . ARG B 1 341 ? 13.383  25.559  8.633   1.00 54.96 ? 342 ARG B NH1 1 
ATOM   5566 N NH2 . ARG B 1 341 ? 12.347  25.570  10.678  1.00 48.67 ? 342 ARG B NH2 1 
ATOM   5567 N N   . ILE B 1 342 ? 11.607  19.934  5.503   1.00 25.04 ? 343 ILE B N   1 
ATOM   5568 C CA  . ILE B 1 342 ? 12.186  20.244  4.196   1.00 26.11 ? 343 ILE B CA  1 
ATOM   5569 C C   . ILE B 1 342 ? 11.705  21.633  3.796   1.00 25.70 ? 343 ILE B C   1 
ATOM   5570 O O   . ILE B 1 342 ? 10.687  22.113  4.312   1.00 26.34 ? 343 ILE B O   1 
ATOM   5571 C CB  . ILE B 1 342 ? 11.799  19.198  3.126   1.00 23.98 ? 343 ILE B CB  1 
ATOM   5572 C CG1 . ILE B 1 342 ? 10.308  19.281  2.789   1.00 25.68 ? 343 ILE B CG1 1 
ATOM   5573 C CG2 . ILE B 1 342 ? 12.158  17.776  3.596   1.00 26.33 ? 343 ILE B CG2 1 
ATOM   5574 C CD1 . ILE B 1 342 ? 9.855   18.218  1.792   1.00 27.89 ? 343 ILE B CD1 1 
ATOM   5575 N N   . PRO B 1 343 ? 12.405  22.294  2.875   1.00 29.72 ? 344 PRO B N   1 
ATOM   5576 C CA  . PRO B 1 343 ? 11.997  23.647  2.479   1.00 24.37 ? 344 PRO B CA  1 
ATOM   5577 C C   . PRO B 1 343 ? 10.531  23.702  2.055   1.00 25.29 ? 344 PRO B C   1 
ATOM   5578 O O   . PRO B 1 343 ? 10.030  22.814  1.357   1.00 22.59 ? 344 PRO B O   1 
ATOM   5579 C CB  . PRO B 1 343 ? 12.934  23.961  1.310   1.00 27.62 ? 344 PRO B CB  1 
ATOM   5580 C CG  . PRO B 1 343 ? 14.168  23.211  1.616   1.00 28.21 ? 344 PRO B CG  1 
ATOM   5581 C CD  . PRO B 1 343 ? 13.637  21.883  2.176   1.00 27.62 ? 344 PRO B CD  1 
ATOM   5582 N N   . ASN B 1 344 ? 9.835   24.754  2.500   1.00 24.46 ? 345 ASN B N   1 
ATOM   5583 C CA  . ASN B 1 344 ? 8.408   24.888  2.189   1.00 25.19 ? 345 ASN B CA  1 
ATOM   5584 C C   . ASN B 1 344 ? 8.161   24.949  0.685   1.00 25.67 ? 345 ASN B C   1 
ATOM   5585 O O   . ASN B 1 344 ? 7.145   24.444  0.197   1.00 24.13 ? 345 ASN B O   1 
ATOM   5586 C CB  . ASN B 1 344 ? 7.836   26.134  2.866   1.00 29.14 ? 345 ASN B CB  1 
ATOM   5587 C CG  . ASN B 1 344 ? 7.652   25.950  4.359   1.00 27.35 ? 345 ASN B CG  1 
ATOM   5588 O OD1 . ASN B 1 344 ? 7.786   24.849  4.868   1.00 30.81 ? 345 ASN B OD1 1 
ATOM   5589 N ND2 . ASN B 1 344 ? 7.331   27.028  5.064   1.00 30.28 ? 345 ASN B ND2 1 
ATOM   5590 N N   . GLU B 1 345 ? 9.073   25.576  -0.060  1.00 24.80 ? 346 GLU B N   1 
ATOM   5591 C CA  . GLU B 1 345 ? 8.934   25.665  -1.511  1.00 21.67 ? 346 GLU B CA  1 
ATOM   5592 C C   . GLU B 1 345 ? 8.942   24.282  -2.166  1.00 25.55 ? 346 GLU B C   1 
ATOM   5593 O O   . GLU B 1 345 ? 8.239   24.056  -3.154  1.00 27.11 ? 346 GLU B O   1 
ATOM   5594 C CB  . GLU B 1 345 ? 10.060  26.549  -2.075  1.00 24.08 ? 346 GLU B CB  1 
ATOM   5595 C CG  . GLU B 1 345 ? 11.462  26.205  -1.526  1.00 32.58 ? 346 GLU B CG  1 
ATOM   5596 C CD  . GLU B 1 345 ? 11.936  27.084  -0.334  1.00 39.93 ? 346 GLU B CD  1 
ATOM   5597 O OE1 . GLU B 1 345 ? 11.165  27.326  0.645   1.00 32.37 ? 346 GLU B OE1 1 
ATOM   5598 O OE2 . GLU B 1 345 ? 13.115  27.525  -0.383  1.00 43.60 ? 346 GLU B OE2 1 
ATOM   5599 N N   . GLU B 1 346 ? 9.726   23.339  -1.633  1.00 22.96 ? 347 GLU B N   1 
ATOM   5600 C CA  . GLU B 1 346 ? 9.711   21.984  -2.201  1.00 25.24 ? 347 GLU B CA  1 
ATOM   5601 C C   . GLU B 1 346 ? 8.362   21.297  -1.985  1.00 24.73 ? 347 GLU B C   1 
ATOM   5602 O O   . GLU B 1 346 ? 7.881   20.575  -2.870  1.00 25.88 ? 347 GLU B O   1 
ATOM   5603 C CB  . GLU B 1 346 ? 10.833  21.132  -1.606  1.00 25.96 ? 347 GLU B CB  1 
ATOM   5604 C CG  . GLU B 1 346 ? 12.232  21.675  -1.864  1.00 26.92 ? 347 GLU B CG  1 
ATOM   5605 C CD  . GLU B 1 346 ? 12.853  21.134  -3.131  1.00 34.90 ? 347 GLU B CD  1 
ATOM   5606 O OE1 . GLU B 1 346 ? 12.101  20.797  -4.079  1.00 34.48 ? 347 GLU B OE1 1 
ATOM   5607 O OE2 . GLU B 1 346 ? 14.103  21.030  -3.170  1.00 33.68 ? 347 GLU B OE2 1 
ATOM   5608 N N   . ARG B 1 347 ? 7.744   21.499  -0.816  1.00 21.52 ? 348 ARG B N   1 
ATOM   5609 C CA  . ARG B 1 347 ? 6.429   20.911  -0.554  1.00 21.64 ? 348 ARG B CA  1 
ATOM   5610 C C   . ARG B 1 347 ? 5.383   21.460  -1.511  1.00 21.01 ? 348 ARG B C   1 
ATOM   5611 O O   . ARG B 1 347 ? 4.590   20.706  -2.081  1.00 21.59 ? 348 ARG B O   1 
ATOM   5612 C CB  . ARG B 1 347 ? 5.996   21.186  0.890   1.00 20.30 ? 348 ARG B CB  1 
ATOM   5613 C CG  . ARG B 1 347 ? 7.089   20.967  1.927   1.00 25.05 ? 348 ARG B CG  1 
ATOM   5614 C CD  . ARG B 1 347 ? 6.624   21.448  3.282   1.00 22.89 ? 348 ARG B CD  1 
ATOM   5615 N NE  . ARG B 1 347 ? 7.743   21.630  4.202   1.00 23.98 ? 348 ARG B NE  1 
ATOM   5616 C CZ  . ARG B 1 347 ? 7.604   21.991  5.470   1.00 23.90 ? 348 ARG B CZ  1 
ATOM   5617 N NH1 . ARG B 1 347 ? 6.404   22.147  6.016   1.00 20.46 ? 348 ARG B NH1 1 
ATOM   5618 N NH2 . ARG B 1 347 ? 8.693   22.196  6.211   1.00 23.90 ? 348 ARG B NH2 1 
ATOM   5619 N N   . ILE B 1 348 ? 5.360   22.786  -1.680  1.00 20.83 ? 349 ILE B N   1 
ATOM   5620 C CA  . ILE B 1 348 ? 4.374   23.437  -2.541  1.00 21.48 ? 349 ILE B CA  1 
ATOM   5621 C C   . ILE B 1 348 ? 4.562   23.011  -3.993  1.00 20.71 ? 349 ILE B C   1 
ATOM   5622 O O   . ILE B 1 348 ? 3.587   22.752  -4.710  1.00 23.15 ? 349 ILE B O   1 
ATOM   5623 C CB  . ILE B 1 348 ? 4.482   24.971  -2.380  1.00 20.19 ? 349 ILE B CB  1 
ATOM   5624 C CG1 . ILE B 1 348 ? 4.115   25.383  -0.947  1.00 20.96 ? 349 ILE B CG1 1 
ATOM   5625 C CG2 . ILE B 1 348 ? 3.632   25.732  -3.444  1.00 21.80 ? 349 ILE B CG2 1 
ATOM   5626 C CD1 . ILE B 1 348 ? 4.532   26.810  -0.580  1.00 21.41 ? 349 ILE B CD1 1 
ATOM   5627 N N   . LYS B 1 349 ? 5.815   22.969  -4.460  1.00 22.17 ? 350 LYS B N   1 
ATOM   5628 C CA  . LYS B 1 349 ? 6.081   22.624  -5.856  1.00 23.04 ? 350 LYS B CA  1 
ATOM   5629 C C   . LYS B 1 349 ? 5.670   21.187  -6.155  1.00 22.88 ? 350 LYS B C   1 
ATOM   5630 O O   . LYS B 1 349 ? 5.079   20.904  -7.205  1.00 26.34 ? 350 LYS B O   1 
ATOM   5631 C CB  . LYS B 1 349 ? 7.567   22.798  -6.180  1.00 26.78 ? 350 LYS B CB  1 
ATOM   5632 C CG  . LYS B 1 349 ? 8.039   24.212  -6.369  1.00 28.29 ? 350 LYS B CG  1 
ATOM   5633 C CD  . LYS B 1 349 ? 9.559   24.236  -6.528  1.00 30.20 ? 350 LYS B CD  1 
ATOM   5634 C CE  . LYS B 1 349 ? 10.082  25.659  -6.651  1.00 41.02 ? 350 LYS B CE  1 
ATOM   5635 N NZ  . LYS B 1 349 ? 11.576  25.691  -6.684  1.00 47.80 ? 350 LYS B NZ  1 
ATOM   5636 N N   . ALA B 1 350 ? 5.984   20.272  -5.247  1.00 22.41 ? 351 ALA B N   1 
ATOM   5637 C CA  . ALA B 1 350 ? 5.692   18.861  -5.478  1.00 22.03 ? 351 ALA B CA  1 
ATOM   5638 C C   . ALA B 1 350 ? 4.188   18.621  -5.511  1.00 23.27 ? 351 ALA B C   1 
ATOM   5639 O O   . ALA B 1 350 ? 3.677   17.934  -6.405  1.00 22.80 ? 351 ALA B O   1 
ATOM   5640 C CB  . ALA B 1 350 ? 6.357   18.012  -4.397  1.00 24.31 ? 351 ALA B CB  1 
ATOM   5641 N N   . ALA B 1 351 ? 3.464   19.194  -4.545  1.00 22.22 ? 352 ALA B N   1 
ATOM   5642 C CA  . ALA B 1 351 ? 2.007   19.070  -4.522  1.00 21.51 ? 352 ALA B CA  1 
ATOM   5643 C C   . ALA B 1 351 ? 1.370   19.691  -5.757  1.00 23.50 ? 352 ALA B C   1 
ATOM   5644 O O   . ALA B 1 351 ? 0.416   19.138  -6.319  1.00 25.91 ? 352 ALA B O   1 
ATOM   5645 C CB  . ALA B 1 351 ? 1.452   19.731  -3.257  1.00 22.75 ? 352 ALA B CB  1 
ATOM   5646 N N   . TYR B 1 352 ? 1.857   20.866  -6.166  1.00 25.01 ? 353 TYR B N   1 
ATOM   5647 C CA  . TYR B 1 352 ? 1.359   21.525  -7.370  1.00 24.92 ? 353 TYR B CA  1 
ATOM   5648 C C   . TYR B 1 352 ? 1.500   20.623  -8.597  1.00 27.57 ? 353 TYR B C   1 
ATOM   5649 O O   . TYR B 1 352 ? 0.575   20.502  -9.409  1.00 29.26 ? 353 TYR B O   1 
ATOM   5650 C CB  . TYR B 1 352 ? 2.125   22.833  -7.566  1.00 25.66 ? 353 TYR B CB  1 
ATOM   5651 C CG  . TYR B 1 352 ? 1.597   23.747  -8.648  1.00 29.13 ? 353 TYR B CG  1 
ATOM   5652 C CD1 . TYR B 1 352 ? 0.584   24.652  -8.374  1.00 27.81 ? 353 TYR B CD1 1 
ATOM   5653 C CD2 . TYR B 1 352 ? 2.131   23.718  -9.934  1.00 27.09 ? 353 TYR B CD2 1 
ATOM   5654 C CE1 . TYR B 1 352 ? 0.108   25.503  -9.348  1.00 33.86 ? 353 TYR B CE1 1 
ATOM   5655 C CE2 . TYR B 1 352 ? 1.653   24.569  -10.924 1.00 30.80 ? 353 TYR B CE2 1 
ATOM   5656 C CZ  . TYR B 1 352 ? 0.639   25.450  -10.621 1.00 33.89 ? 353 TYR B CZ  1 
ATOM   5657 O OH  . TYR B 1 352 ? 0.151   26.302  -11.585 1.00 42.80 ? 353 TYR B OH  1 
ATOM   5658 N N   . ALA B 1 353 ? 2.668   20.003  -8.764  1.00 26.53 ? 354 ALA B N   1 
ATOM   5659 C CA  . ALA B 1 353 ? 2.872   19.122  -9.911  1.00 29.22 ? 354 ALA B CA  1 
ATOM   5660 C C   . ALA B 1 353 ? 1.913   17.938  -9.880  1.00 27.76 ? 354 ALA B C   1 
ATOM   5661 O O   . ALA B 1 353 ? 1.340   17.568  -10.909 1.00 28.55 ? 354 ALA B O   1 
ATOM   5662 C CB  . ALA B 1 353 ? 4.324   18.642  -9.949  1.00 28.29 ? 354 ALA B CB  1 
ATOM   5663 N N   . VAL B 1 354 ? 1.716   17.329  -8.710  1.00 26.89 ? 355 VAL B N   1 
ATOM   5664 C CA  . VAL B 1 354 ? 0.812   16.182  -8.629  1.00 28.82 ? 355 VAL B CA  1 
ATOM   5665 C C   . VAL B 1 354 ? -0.622  16.603  -8.940  1.00 29.95 ? 355 VAL B C   1 
ATOM   5666 O O   . VAL B 1 354 ? -1.270  16.049  -9.833  1.00 27.21 ? 355 VAL B O   1 
ATOM   5667 C CB  . VAL B 1 354 ? 0.920   15.513  -7.249  1.00 26.11 ? 355 VAL B CB  1 
ATOM   5668 C CG1 . VAL B 1 354 ? -0.197  14.500  -7.057  1.00 27.09 ? 355 VAL B CG1 1 
ATOM   5669 C CG2 . VAL B 1 354 ? 2.276   14.853  -7.116  1.00 24.97 ? 355 VAL B CG2 1 
ATOM   5670 N N   . LEU B 1 355 ? -1.128  17.618  -8.238  1.00 27.70 ? 356 LEU B N   1 
ATOM   5671 C CA  . LEU B 1 355 ? -2.543  17.951  -8.384  1.00 28.54 ? 356 LEU B CA  1 
ATOM   5672 C C   . LEU B 1 355 ? -2.875  18.421  -9.798  1.00 32.77 ? 356 LEU B C   1 
ATOM   5673 O O   . LEU B 1 355 ? -3.963  18.132  -10.307 1.00 33.10 ? 356 LEU B O   1 
ATOM   5674 C CB  . LEU B 1 355 ? -2.944  19.001  -7.344  1.00 30.40 ? 356 LEU B CB  1 
ATOM   5675 C CG  . LEU B 1 355 ? -2.937  18.454  -5.910  1.00 26.38 ? 356 LEU B CG  1 
ATOM   5676 C CD1 . LEU B 1 355 ? -3.266  19.556  -4.937  1.00 29.26 ? 356 LEU B CD1 1 
ATOM   5677 C CD2 . LEU B 1 355 ? -3.920  17.305  -5.760  1.00 30.13 ? 356 LEU B CD2 1 
ATOM   5678 N N   . ASN B 1 356 ? -1.951  19.114  -10.459 1.00 28.89 ? 357 ASN B N   1 
ATOM   5679 C CA  . ASN B 1 356 ? -2.233  19.587  -11.806 1.00 34.04 ? 357 ASN B CA  1 
ATOM   5680 C C   . ASN B 1 356 ? -2.132  18.492  -12.860 1.00 35.72 ? 357 ASN B C   1 
ATOM   5681 O O   . ASN B 1 356 ? -2.719  18.641  -13.937 1.00 35.72 ? 357 ASN B O   1 
ATOM   5682 C CB  . ASN B 1 356 ? -1.308  20.744  -12.145 1.00 30.44 ? 357 ASN B CB  1 
ATOM   5683 C CG  . ASN B 1 356 ? -1.823  22.047  -11.599 1.00 37.80 ? 357 ASN B CG  1 
ATOM   5684 O OD1 . ASN B 1 356 ? -2.652  22.705  -12.230 1.00 43.00 ? 357 ASN B OD1 1 
ATOM   5685 N ND2 . ASN B 1 356 ? -1.370  22.414  -10.403 1.00 38.41 ? 357 ASN B ND2 1 
ATOM   5686 N N   . ALA B 1 357 ? -1.429  17.395  -12.573 1.00 35.29 ? 358 ALA B N   1 
ATOM   5687 C CA  . ALA B 1 357 ? -1.345  16.284  -13.517 1.00 35.24 ? 358 ALA B CA  1 
ATOM   5688 C C   . ALA B 1 357 ? -2.546  15.350  -13.450 1.00 40.78 ? 358 ALA B C   1 
ATOM   5689 O O   . ALA B 1 357 ? -2.711  14.518  -14.349 1.00 41.31 ? 358 ALA B O   1 
ATOM   5690 C CB  . ALA B 1 357 ? -0.060  15.484  -13.285 1.00 34.72 ? 358 ALA B CB  1 
ATOM   5691 N N   . ILE B 1 358 ? -3.384  15.464  -12.427 1.00 37.53 ? 359 ILE B N   1 
ATOM   5692 C CA  . ILE B 1 358 ? -4.562  14.613  -12.297 1.00 43.15 ? 359 ILE B CA  1 
ATOM   5693 C C   . ILE B 1 358 ? -5.741  15.225  -13.051 1.00 42.75 ? 359 ILE B C   1 
ATOM   5694 O O   . ILE B 1 358 ? -6.106  16.384  -12.819 1.00 46.54 ? 359 ILE B O   1 
ATOM   5695 C CB  . ILE B 1 358 ? -4.914  14.376  -10.808 1.00 40.13 ? 359 ILE B CB  1 
ATOM   5696 C CG1 . ILE B 1 358 ? -3.807  13.572  -10.119 1.00 37.68 ? 359 ILE B CG1 1 
ATOM   5697 C CG2 . ILE B 1 358 ? -6.259  13.681  -10.680 1.00 43.87 ? 359 ILE B CG2 1 
ATOM   5698 C CD1 . ILE B 1 358 ? -3.954  13.472  -8.604  1.00 34.51 ? 359 ILE B CD1 1 
HETATM 5699 N N   . NO3 C 2 .   ? 14.815  17.797  11.339  1.00 39.56 ? 401 NO3 B N   1 
HETATM 5700 O O1  . NO3 C 2 .   ? 15.281  18.895  10.990  1.00 34.85 ? 401 NO3 B O1  1 
HETATM 5701 O O2  . NO3 C 2 .   ? 15.579  16.866  11.622  1.00 39.22 ? 401 NO3 B O2  1 
HETATM 5702 O O3  . NO3 C 2 .   ? 13.582  17.623  11.402  1.00 40.52 ? 401 NO3 B O3  1 
HETATM 5703 C C1  . EDO D 3 .   ? 16.212  22.409  4.311   1.00 39.03 ? 402 EDO B C1  1 
HETATM 5704 O O1  . EDO D 3 .   ? 17.182  21.456  4.670   1.00 42.95 ? 402 EDO B O1  1 
HETATM 5705 C C2  . EDO D 3 .   ? 15.502  22.942  5.530   1.00 40.17 ? 402 EDO B C2  1 
HETATM 5706 O O2  . EDO D 3 .   ? 14.120  22.696  5.403   1.00 38.39 ? 402 EDO B O2  1 
HETATM 5707 C C1  . EDO E 3 .   ? 7.594   46.679  3.926   1.00 30.06 ? 403 EDO B C1  1 
HETATM 5708 O O1  . EDO E 3 .   ? 8.851   46.791  3.267   1.00 36.20 ? 403 EDO B O1  1 
HETATM 5709 C C2  . EDO E 3 .   ? 7.797   46.556  5.421   1.00 30.60 ? 403 EDO B C2  1 
HETATM 5710 O O2  . EDO E 3 .   ? 8.101   45.207  5.779   1.00 35.56 ? 403 EDO B O2  1 
HETATM 5711 O O   . HOH F 4 .   ? 42.833  -21.250 9.349   1.00 53.15 ? 401 HOH A O   1 
HETATM 5712 O O   . HOH F 4 .   ? 45.838  -35.746 -2.637  1.00 32.01 ? 402 HOH A O   1 
HETATM 5713 O O   . HOH F 4 .   ? 24.187  -9.060  18.800  1.00 42.79 ? 403 HOH A O   1 
HETATM 5714 O O   . HOH F 4 .   ? 4.931   -22.506 -4.679  1.00 32.10 ? 404 HOH A O   1 
HETATM 5715 O O   . HOH F 4 .   ? 37.432  -32.397 -23.049 1.00 39.36 ? 405 HOH A O   1 
HETATM 5716 O O   . HOH F 4 .   ? 21.270  -36.190 5.149   1.00 20.80 ? 406 HOH A O   1 
HETATM 5717 O O   . HOH F 4 .   ? 8.134   -4.974  -0.457  1.00 38.34 ? 407 HOH A O   1 
HETATM 5718 O O   . HOH F 4 .   ? 14.413  -46.327 -8.635  1.00 43.37 ? 408 HOH A O   1 
HETATM 5719 O O   . HOH F 4 .   ? 19.449  1.607   -3.373  1.00 40.44 ? 409 HOH A O   1 
HETATM 5720 O O   . HOH F 4 .   ? 24.608  -24.065 24.505  1.00 26.37 ? 410 HOH A O   1 
HETATM 5721 O O   . HOH F 4 .   ? 28.094  -25.408 5.166   1.00 41.99 ? 411 HOH A O   1 
HETATM 5722 O O   . HOH F 4 .   ? 34.981  -30.513 -2.625  1.00 19.58 ? 412 HOH A O   1 
HETATM 5723 O O   . HOH F 4 .   ? 16.497  -31.748 18.973  1.00 29.42 ? 413 HOH A O   1 
HETATM 5724 O O   . HOH F 4 .   ? 32.403  -39.603 2.558   1.00 27.55 ? 414 HOH A O   1 
HETATM 5725 O O   . HOH F 4 .   ? 20.608  -16.026 -3.558  1.00 26.46 ? 415 HOH A O   1 
HETATM 5726 O O   . HOH F 4 .   ? 30.827  -33.602 -24.851 1.00 32.48 ? 416 HOH A O   1 
HETATM 5727 O O   . HOH F 4 .   ? 26.355  -27.743 3.929   1.00 26.62 ? 417 HOH A O   1 
HETATM 5728 O O   . HOH F 4 .   ? 4.294   -15.586 -7.390  1.00 41.45 ? 418 HOH A O   1 
HETATM 5729 O O   . HOH F 4 .   ? 5.674   -31.337 -10.023 1.00 37.80 ? 419 HOH A O   1 
HETATM 5730 O O   . HOH F 4 .   ? 20.639  -15.873 26.013  1.00 31.97 ? 420 HOH A O   1 
HETATM 5731 O O   . HOH F 4 .   ? 15.996  -0.848  20.658  1.00 43.64 ? 421 HOH A O   1 
HETATM 5732 O O   . HOH F 4 .   ? 34.998  -29.599 -24.652 1.00 34.25 ? 422 HOH A O   1 
HETATM 5733 O O   . HOH F 4 .   ? 47.731  -30.573 -5.686  1.00 23.48 ? 423 HOH A O   1 
HETATM 5734 O O   . HOH F 4 .   ? 13.669  -3.301  -4.049  1.00 32.86 ? 424 HOH A O   1 
HETATM 5735 O O   . HOH F 4 .   ? 33.824  -19.016 -12.856 1.00 34.66 ? 425 HOH A O   1 
HETATM 5736 O O   . HOH F 4 .   ? 26.625  -27.168 -18.696 1.00 35.49 ? 426 HOH A O   1 
HETATM 5737 O O   . HOH F 4 .   ? 10.555  -23.840 22.695  1.00 36.03 ? 427 HOH A O   1 
HETATM 5738 O O   . HOH F 4 .   ? 26.069  -10.718 17.365  1.00 31.07 ? 428 HOH A O   1 
HETATM 5739 O O   . HOH F 4 .   ? 39.589  -36.757 -5.922  1.00 20.17 ? 429 HOH A O   1 
HETATM 5740 O O   . HOH F 4 .   ? 36.120  -17.769 -20.187 1.00 42.53 ? 430 HOH A O   1 
HETATM 5741 O O   . HOH F 4 .   ? 5.627   -14.888 1.624   1.00 35.00 ? 431 HOH A O   1 
HETATM 5742 O O   . HOH F 4 .   ? 28.242  -32.090 17.956  1.00 25.92 ? 432 HOH A O   1 
HETATM 5743 O O   . HOH F 4 .   ? 42.272  -31.962 -15.191 1.00 31.51 ? 433 HOH A O   1 
HETATM 5744 O O   . HOH F 4 .   ? 36.918  -46.455 -13.832 1.00 31.14 ? 434 HOH A O   1 
HETATM 5745 O O   . HOH F 4 .   ? 8.110   -21.351 -12.749 1.00 36.86 ? 435 HOH A O   1 
HETATM 5746 O O   . HOH F 4 .   ? 25.762  -32.029 22.968  1.00 29.71 ? 436 HOH A O   1 
HETATM 5747 O O   . HOH F 4 .   ? 44.322  -38.076 -10.936 1.00 28.80 ? 437 HOH A O   1 
HETATM 5748 O O   . HOH F 4 .   ? 38.615  -30.870 -3.082  1.00 23.20 ? 438 HOH A O   1 
HETATM 5749 O O   . HOH F 4 .   ? 25.393  -30.603 1.474   1.00 25.73 ? 439 HOH A O   1 
HETATM 5750 O O   . HOH F 4 .   ? 34.315  -25.404 -23.402 1.00 24.48 ? 440 HOH A O   1 
HETATM 5751 O O   . HOH F 4 .   ? 11.780  -19.940 -13.398 1.00 32.18 ? 441 HOH A O   1 
HETATM 5752 O O   . HOH F 4 .   ? 29.063  -28.460 21.722  1.00 26.77 ? 442 HOH A O   1 
HETATM 5753 O O   . HOH F 4 .   ? 19.262  -38.046 -18.423 1.00 36.20 ? 443 HOH A O   1 
HETATM 5754 O O   . HOH F 4 .   ? 36.295  -24.686 0.411   1.00 27.07 ? 444 HOH A O   1 
HETATM 5755 O O   . HOH F 4 .   ? 36.110  -25.203 -19.301 1.00 27.75 ? 445 HOH A O   1 
HETATM 5756 O O   . HOH F 4 .   ? 38.758  -29.914 -15.056 1.00 23.63 ? 446 HOH A O   1 
HETATM 5757 O O   . HOH F 4 .   ? 31.741  -21.113 -8.706  1.00 23.18 ? 447 HOH A O   1 
HETATM 5758 O O   . HOH F 4 .   ? 12.830  -32.359 12.997  1.00 27.90 ? 448 HOH A O   1 
HETATM 5759 O O   . HOH F 4 .   ? 17.287  -24.106 -14.389 1.00 31.84 ? 449 HOH A O   1 
HETATM 5760 O O   . HOH F 4 .   ? 33.418  -32.282 -3.880  1.00 17.54 ? 450 HOH A O   1 
HETATM 5761 O O   . HOH F 4 .   ? 7.733   -40.651 -14.136 1.00 39.46 ? 451 HOH A O   1 
HETATM 5762 O O   . HOH F 4 .   ? 2.817   -14.164 16.611  1.00 42.28 ? 452 HOH A O   1 
HETATM 5763 O O   . HOH F 4 .   ? 32.506  -43.053 -5.649  1.00 20.95 ? 453 HOH A O   1 
HETATM 5764 O O   . HOH F 4 .   ? 29.108  -42.320 7.948   1.00 30.30 ? 454 HOH A O   1 
HETATM 5765 O O   . HOH F 4 .   ? 36.134  -26.713 3.186   1.00 28.39 ? 455 HOH A O   1 
HETATM 5766 O O   . HOH F 4 .   ? 3.676   -37.226 -7.313  1.00 37.43 ? 456 HOH A O   1 
HETATM 5767 O O   . HOH F 4 .   ? 36.248  -36.118 -15.522 1.00 20.71 ? 457 HOH A O   1 
HETATM 5768 O O   . HOH F 4 .   ? 9.366   -17.680 -11.578 1.00 27.44 ? 458 HOH A O   1 
HETATM 5769 O O   . HOH F 4 .   ? 13.692  -33.545 28.608  1.00 41.07 ? 459 HOH A O   1 
HETATM 5770 O O   . HOH F 4 .   ? 31.516  -27.636 14.941  1.00 33.13 ? 460 HOH A O   1 
HETATM 5771 O O   . HOH F 4 .   ? 8.589   -40.489 -1.968  1.00 25.02 ? 461 HOH A O   1 
HETATM 5772 O O   . HOH F 4 .   ? -1.071  -33.197 8.415   1.00 29.19 ? 462 HOH A O   1 
HETATM 5773 O O   . HOH F 4 .   ? 27.639  -43.974 -16.102 1.00 34.95 ? 463 HOH A O   1 
HETATM 5774 O O   . HOH F 4 .   ? 28.811  -40.176 -23.709 1.00 37.54 ? 464 HOH A O   1 
HETATM 5775 O O   . HOH F 4 .   ? 29.356  -16.266 -16.096 1.00 40.58 ? 465 HOH A O   1 
HETATM 5776 O O   . HOH F 4 .   ? 4.481   -9.743  10.192  1.00 41.68 ? 466 HOH A O   1 
HETATM 5777 O O   . HOH F 4 .   ? 30.472  -38.039 1.361   1.00 21.61 ? 467 HOH A O   1 
HETATM 5778 O O   . HOH F 4 .   ? 27.519  -30.137 19.896  1.00 27.82 ? 468 HOH A O   1 
HETATM 5779 O O   . HOH F 4 .   ? 20.486  0.717   8.962   1.00 39.97 ? 469 HOH A O   1 
HETATM 5780 O O   . HOH F 4 .   ? 6.778   -21.913 -6.634  1.00 28.32 ? 470 HOH A O   1 
HETATM 5781 O O   . HOH F 4 .   ? 37.904  -36.639 -0.892  1.00 18.75 ? 471 HOH A O   1 
HETATM 5782 O O   . HOH F 4 .   ? 10.331  -10.695 4.140   1.00 21.78 ? 472 HOH A O   1 
HETATM 5783 O O   . HOH F 4 .   ? 29.263  -5.554  5.936   1.00 43.78 ? 473 HOH A O   1 
HETATM 5784 O O   . HOH F 4 .   ? 3.949   -35.958 -5.035  1.00 32.62 ? 474 HOH A O   1 
HETATM 5785 O O   . HOH F 4 .   ? 4.086   -10.988 -0.990  1.00 35.03 ? 475 HOH A O   1 
HETATM 5786 O O   . HOH F 4 .   ? 39.433  -35.957 -17.386 1.00 26.46 ? 476 HOH A O   1 
HETATM 5787 O O   . HOH F 4 .   ? 13.459  -40.078 4.490   1.00 25.59 ? 477 HOH A O   1 
HETATM 5788 O O   . HOH F 4 .   ? 32.209  -41.899 0.563   1.00 27.67 ? 478 HOH A O   1 
HETATM 5789 O O   . HOH F 4 .   ? 40.091  -41.873 -5.199  1.00 21.50 ? 479 HOH A O   1 
HETATM 5790 O O   . HOH F 4 .   ? 4.623   -18.380 3.920   1.00 32.33 ? 480 HOH A O   1 
HETATM 5791 O O   . HOH F 4 .   ? 27.985  -24.024 -8.660  1.00 23.59 ? 481 HOH A O   1 
HETATM 5792 O O   . HOH F 4 .   ? 6.987   -19.834 -4.343  1.00 28.85 ? 482 HOH A O   1 
HETATM 5793 O O   . HOH F 4 .   ? 17.124  -31.297 -16.587 1.00 28.69 ? 483 HOH A O   1 
HETATM 5794 O O   A HOH F 4 .   ? 7.225   -3.572  7.702   0.52 25.05 ? 484 HOH A O   1 
HETATM 5795 O O   B HOH F 4 .   ? 5.367   -3.007  6.924   0.48 30.61 ? 484 HOH A O   1 
HETATM 5796 O O   . HOH F 4 .   ? 7.976   -20.043 -7.412  1.00 31.70 ? 485 HOH A O   1 
HETATM 5797 O O   . HOH F 4 .   ? 41.926  -33.912 -18.564 1.00 35.60 ? 486 HOH A O   1 
HETATM 5798 O O   . HOH F 4 .   ? 18.447  -2.349  20.569  1.00 37.24 ? 487 HOH A O   1 
HETATM 5799 O O   . HOH F 4 .   ? 35.849  -28.921 5.358   1.00 25.48 ? 488 HOH A O   1 
HETATM 5800 O O   . HOH F 4 .   ? 36.555  -32.813 -1.710  1.00 17.55 ? 489 HOH A O   1 
HETATM 5801 O O   . HOH F 4 .   ? 1.720   -17.805 13.743  1.00 38.52 ? 490 HOH A O   1 
HETATM 5802 O O   . HOH F 4 .   ? 18.414  1.152   7.826   1.00 39.17 ? 491 HOH A O   1 
HETATM 5803 O O   . HOH F 4 .   ? 21.069  -0.428  14.867  1.00 41.64 ? 492 HOH A O   1 
HETATM 5804 O O   . HOH F 4 .   ? 16.325  7.577   -0.748  1.00 42.36 ? 493 HOH A O   1 
HETATM 5805 O O   . HOH F 4 .   ? 34.510  -43.377 -15.305 1.00 27.37 ? 494 HOH A O   1 
HETATM 5806 O O   . HOH F 4 .   ? 15.226  -40.756 -13.234 1.00 26.39 ? 495 HOH A O   1 
HETATM 5807 O O   . HOH F 4 .   ? 37.305  -36.852 -20.729 1.00 31.86 ? 496 HOH A O   1 
HETATM 5808 O O   . HOH F 4 .   ? 24.442  -42.363 3.657   1.00 28.60 ? 497 HOH A O   1 
HETATM 5809 O O   . HOH F 4 .   ? 20.247  -43.863 -2.266  1.00 22.42 ? 498 HOH A O   1 
HETATM 5810 O O   . HOH F 4 .   ? 25.815  -14.864 22.160  1.00 35.86 ? 499 HOH A O   1 
HETATM 5811 O O   . HOH F 4 .   ? 9.702   -2.178  10.032  1.00 24.16 ? 500 HOH A O   1 
HETATM 5812 O O   . HOH F 4 .   ? 28.549  -45.392 -5.228  1.00 27.70 ? 501 HOH A O   1 
HETATM 5813 O O   . HOH F 4 .   ? 40.818  -19.226 -11.342 1.00 34.42 ? 502 HOH A O   1 
HETATM 5814 O O   . HOH F 4 .   ? 19.211  -29.408 -16.776 1.00 38.71 ? 503 HOH A O   1 
HETATM 5815 O O   . HOH F 4 .   ? 18.521  -9.581  -1.083  1.00 32.74 ? 504 HOH A O   1 
HETATM 5816 O O   . HOH F 4 .   ? 18.955  -27.560 -14.926 1.00 26.95 ? 505 HOH A O   1 
HETATM 5817 O O   . HOH F 4 .   ? 11.052  -2.153  7.967   1.00 24.89 ? 506 HOH A O   1 
HETATM 5818 O O   . HOH F 4 .   ? 22.944  -24.899 21.013  1.00 28.33 ? 507 HOH A O   1 
HETATM 5819 O O   . HOH F 4 .   ? 39.241  -29.064 -9.856  1.00 25.47 ? 508 HOH A O   1 
HETATM 5820 O O   . HOH F 4 .   ? 6.366   -11.316 -1.923  1.00 22.87 ? 509 HOH A O   1 
HETATM 5821 O O   . HOH F 4 .   ? 3.124   -37.666 -1.212  1.00 28.64 ? 510 HOH A O   1 
HETATM 5822 O O   . HOH F 4 .   ? 23.203  -19.999 16.698  1.00 27.52 ? 511 HOH A O   1 
HETATM 5823 O O   . HOH F 4 .   ? 14.841  -29.701 4.328   1.00 21.60 ? 512 HOH A O   1 
HETATM 5824 O O   . HOH F 4 .   ? 27.183  -22.225 -23.024 1.00 30.80 ? 513 HOH A O   1 
HETATM 5825 O O   . HOH F 4 .   ? 22.777  -36.120 21.759  1.00 31.39 ? 514 HOH A O   1 
HETATM 5826 O O   . HOH F 4 .   ? 34.356  -17.228 -21.776 1.00 36.53 ? 515 HOH A O   1 
HETATM 5827 O O   . HOH F 4 .   ? -0.326  -13.145 18.554  1.00 53.20 ? 516 HOH A O   1 
HETATM 5828 O O   . HOH F 4 .   ? 28.360  -21.774 25.173  1.00 31.29 ? 517 HOH A O   1 
HETATM 5829 O O   . HOH F 4 .   ? 38.385  -23.714 -1.849  1.00 32.78 ? 518 HOH A O   1 
HETATM 5830 O O   . HOH F 4 .   ? 7.050   -1.254  2.574   1.00 34.13 ? 519 HOH A O   1 
HETATM 5831 O O   . HOH F 4 .   ? 40.520  -21.786 11.236  1.00 43.61 ? 520 HOH A O   1 
HETATM 5832 O O   . HOH F 4 .   ? 25.690  -44.945 -11.864 1.00 23.10 ? 521 HOH A O   1 
HETATM 5833 O O   . HOH F 4 .   ? 37.770  -21.427 -5.331  1.00 28.59 ? 522 HOH A O   1 
HETATM 5834 O O   . HOH F 4 .   ? 7.774   1.488   2.576   1.00 25.92 ? 523 HOH A O   1 
HETATM 5835 O O   . HOH F 4 .   ? 2.981   -7.580  -3.928  1.00 37.59 ? 524 HOH A O   1 
HETATM 5836 O O   . HOH F 4 .   ? 8.253   -44.153 -7.445  1.00 31.91 ? 525 HOH A O   1 
HETATM 5837 O O   . HOH F 4 .   ? 10.016  -38.357 -2.378  1.00 22.43 ? 526 HOH A O   1 
HETATM 5838 O O   . HOH F 4 .   ? 18.913  -23.926 -4.833  1.00 30.64 ? 527 HOH A O   1 
HETATM 5839 O O   . HOH F 4 .   ? 16.699  -34.372 18.267  1.00 30.17 ? 528 HOH A O   1 
HETATM 5840 O O   . HOH F 4 .   ? 5.142   -6.293  7.178   1.00 29.19 ? 529 HOH A O   1 
HETATM 5841 O O   . HOH F 4 .   ? 6.006   -21.192 -11.511 1.00 42.04 ? 530 HOH A O   1 
HETATM 5842 O O   . HOH F 4 .   ? 26.727  -23.552 7.560   1.00 31.95 ? 531 HOH A O   1 
HETATM 5843 O O   . HOH F 4 .   ? 22.040  -22.663 -12.653 1.00 29.74 ? 532 HOH A O   1 
HETATM 5844 O O   . HOH F 4 .   ? 22.586  -36.103 -21.110 1.00 33.76 ? 533 HOH A O   1 
HETATM 5845 O O   . HOH F 4 .   ? 8.863   2.976   -2.039  1.00 33.04 ? 534 HOH A O   1 
HETATM 5846 O O   . HOH F 4 .   ? 38.706  -43.734 -2.181  1.00 36.97 ? 535 HOH A O   1 
HETATM 5847 O O   . HOH F 4 .   ? 41.443  -31.822 -12.620 1.00 22.08 ? 536 HOH A O   1 
HETATM 5848 O O   . HOH F 4 .   ? 43.488  -31.559 -11.298 1.00 32.11 ? 537 HOH A O   1 
HETATM 5849 O O   . HOH F 4 .   ? 24.966  -30.848 -22.101 1.00 40.57 ? 538 HOH A O   1 
HETATM 5850 O O   . HOH F 4 .   ? 36.782  -22.190 -20.035 1.00 40.48 ? 539 HOH A O   1 
HETATM 5851 O O   . HOH F 4 .   ? 4.827   -11.328 14.595  1.00 31.88 ? 540 HOH A O   1 
HETATM 5852 O O   . HOH F 4 .   ? 8.263   -5.514  12.750  1.00 29.32 ? 541 HOH A O   1 
HETATM 5853 O O   . HOH F 4 .   ? 6.908   -25.582 14.630  1.00 39.28 ? 542 HOH A O   1 
HETATM 5854 O O   . HOH F 4 .   ? 13.285  -23.422 24.090  1.00 44.63 ? 543 HOH A O   1 
HETATM 5855 O O   . HOH F 4 .   ? 10.651  -1.089  -4.443  1.00 39.51 ? 544 HOH A O   1 
HETATM 5856 O O   . HOH F 4 .   ? 19.521  -10.969 25.521  1.00 43.78 ? 545 HOH A O   1 
HETATM 5857 O O   . HOH F 4 .   ? 44.045  -38.558 -0.029  1.00 33.30 ? 546 HOH A O   1 
HETATM 5858 O O   . HOH F 4 .   ? 31.208  -22.060 24.345  1.00 31.68 ? 547 HOH A O   1 
HETATM 5859 O O   . HOH F 4 .   ? 29.477  -22.473 -29.408 1.00 26.99 ? 548 HOH A O   1 
HETATM 5860 O O   . HOH F 4 .   ? 31.758  -25.038 5.354   1.00 34.19 ? 549 HOH A O   1 
HETATM 5861 O O   . HOH F 4 .   ? 17.237  -44.182 -11.618 1.00 39.62 ? 550 HOH A O   1 
HETATM 5862 O O   . HOH F 4 .   ? 22.579  -26.390 -16.772 1.00 43.49 ? 551 HOH A O   1 
HETATM 5863 O O   . HOH F 4 .   ? 38.569  -27.117 -8.402  1.00 27.93 ? 552 HOH A O   1 
HETATM 5864 O O   . HOH F 4 .   ? 19.818  -38.220 24.897  1.00 37.33 ? 553 HOH A O   1 
HETATM 5865 O O   . HOH F 4 .   ? 36.621  -19.324 -24.047 1.00 41.68 ? 554 HOH A O   1 
HETATM 5866 O O   . HOH F 4 .   ? 7.096   -18.827 -10.092 1.00 40.10 ? 555 HOH A O   1 
HETATM 5867 O O   . HOH F 4 .   ? 14.337  -30.593 -19.099 1.00 39.91 ? 556 HOH A O   1 
HETATM 5868 O O   . HOH F 4 .   ? 35.132  -41.988 4.459   1.00 43.13 ? 557 HOH A O   1 
HETATM 5869 O O   . HOH F 4 .   ? 26.058  -28.018 -21.157 1.00 41.41 ? 558 HOH A O   1 
HETATM 5870 O O   . HOH F 4 .   ? 38.240  -39.108 -20.037 1.00 31.52 ? 559 HOH A O   1 
HETATM 5871 O O   . HOH F 4 .   ? 20.539  -14.279 -5.696  1.00 46.37 ? 560 HOH A O   1 
HETATM 5872 O O   . HOH F 4 .   ? 9.697   -36.303 -10.365 1.00 39.34 ? 561 HOH A O   1 
HETATM 5873 O O   . HOH F 4 .   ? 38.333  -26.658 -18.172 1.00 34.70 ? 562 HOH A O   1 
HETATM 5874 O O   . HOH F 4 .   ? 16.137  -32.251 -18.839 1.00 38.92 ? 563 HOH A O   1 
HETATM 5875 O O   . HOH F 4 .   ? 29.156  -21.745 -8.865  1.00 25.96 ? 564 HOH A O   1 
HETATM 5876 O O   . HOH F 4 .   ? 35.564  -16.854 -24.278 1.00 39.61 ? 565 HOH A O   1 
HETATM 5877 O O   . HOH F 4 .   ? 21.294  -26.905 -13.125 1.00 32.53 ? 566 HOH A O   1 
HETATM 5878 O O   . HOH F 4 .   ? 21.895  -36.257 24.223  1.00 37.27 ? 567 HOH A O   1 
HETATM 5879 O O   . HOH F 4 .   ? 1.898   -15.483 11.244  1.00 44.90 ? 568 HOH A O   1 
HETATM 5880 O O   . HOH F 4 .   ? 36.532  -24.509 -22.629 1.00 36.76 ? 569 HOH A O   1 
HETATM 5881 O O   . HOH F 4 .   ? 5.602   -1.582  5.014   1.00 34.06 ? 570 HOH A O   1 
HETATM 5882 O O   . HOH F 4 .   ? 32.286  -41.222 4.952   1.00 34.28 ? 571 HOH A O   1 
HETATM 5883 O O   . HOH F 4 .   ? 16.697  6.299   7.876   1.00 39.60 ? 572 HOH A O   1 
HETATM 5884 O O   . HOH F 4 .   ? 13.372  -42.820 -13.328 1.00 42.50 ? 573 HOH A O   1 
HETATM 5885 O O   . HOH F 4 .   ? 39.833  -29.512 -12.350 1.00 26.15 ? 574 HOH A O   1 
HETATM 5886 O O   . HOH F 4 .   ? 37.497  -29.915 -24.798 1.00 35.87 ? 575 HOH A O   1 
HETATM 5887 O O   . HOH F 4 .   ? 29.272  -40.509 1.057   1.00 29.08 ? 576 HOH A O   1 
HETATM 5888 O O   . HOH F 4 .   ? 25.118  -15.588 24.559  1.00 30.26 ? 577 HOH A O   1 
HETATM 5889 O O   . HOH F 4 .   ? 39.162  -25.662 -22.164 1.00 38.82 ? 578 HOH A O   1 
HETATM 5890 O O   . HOH F 4 .   ? 6.034   -5.225  11.396  1.00 38.44 ? 579 HOH A O   1 
HETATM 5891 O O   . HOH F 4 .   ? 41.365  -27.583 -12.469 1.00 39.68 ? 580 HOH A O   1 
HETATM 5892 O O   . HOH F 4 .   ? 35.791  -48.540 -24.941 1.00 44.22 ? 581 HOH A O   1 
HETATM 5893 O O   . HOH G 4 .   ? -5.100  15.412  26.439  1.00 40.72 ? 501 HOH B O   1 
HETATM 5894 O O   . HOH G 4 .   ? 9.441   6.936   16.013  1.00 34.60 ? 502 HOH B O   1 
HETATM 5895 O O   . HOH G 4 .   ? 2.312   32.129  5.111   1.00 36.03 ? 503 HOH B O   1 
HETATM 5896 O O   . HOH G 4 .   ? 7.232   2.653   0.082   1.00 26.64 ? 504 HOH B O   1 
HETATM 5897 O O   . HOH G 4 .   ? 15.989  19.290  5.215   1.00 32.21 ? 505 HOH B O   1 
HETATM 5898 O O   . HOH G 4 .   ? 5.990   31.072  21.451  1.00 36.05 ? 506 HOH B O   1 
HETATM 5899 O O   . HOH G 4 .   ? 5.682   -0.756  10.983  1.00 34.66 ? 507 HOH B O   1 
HETATM 5900 O O   . HOH G 4 .   ? 8.496   35.146  -3.042  1.00 40.29 ? 508 HOH B O   1 
HETATM 5901 O O   . HOH G 4 .   ? 2.712   19.508  16.334  1.00 25.37 ? 509 HOH B O   1 
HETATM 5902 O O   . HOH G 4 .   ? 7.514   5.602   18.551  1.00 36.44 ? 510 HOH B O   1 
HETATM 5903 O O   . HOH G 4 .   ? 3.605   2.012   13.545  1.00 32.80 ? 511 HOH B O   1 
HETATM 5904 O O   . HOH G 4 .   ? -8.150  43.234  10.031  1.00 28.40 ? 512 HOH B O   1 
HETATM 5905 O O   . HOH G 4 .   ? 5.761   37.667  -0.639  1.00 37.06 ? 513 HOH B O   1 
HETATM 5906 O O   . HOH G 4 .   ? -11.848 42.474  5.441   1.00 33.28 ? 514 HOH B O   1 
HETATM 5907 O O   . HOH G 4 .   ? -14.908 40.525  14.364  1.00 36.94 ? 515 HOH B O   1 
HETATM 5908 O O   . HOH G 4 .   ? 0.255   34.780  -2.374  1.00 26.80 ? 516 HOH B O   1 
HETATM 5909 O O   . HOH G 4 .   ? -7.716  11.873  20.507  1.00 41.72 ? 517 HOH B O   1 
HETATM 5910 O O   . HOH G 4 .   ? -0.502  51.761  7.346   1.00 26.65 ? 518 HOH B O   1 
HETATM 5911 O O   . HOH G 4 .   ? -0.513  46.855  29.636  1.00 36.96 ? 519 HOH B O   1 
HETATM 5912 O O   . HOH G 4 .   ? -15.526 22.958  0.324   1.00 29.85 ? 520 HOH B O   1 
HETATM 5913 O O   . HOH G 4 .   ? -11.248 26.338  29.548  1.00 47.48 ? 521 HOH B O   1 
HETATM 5914 O O   . HOH G 4 .   ? -2.239  5.415   14.978  1.00 27.91 ? 522 HOH B O   1 
HETATM 5915 O O   . HOH G 4 .   ? -8.056  40.688  11.427  1.00 23.69 ? 523 HOH B O   1 
HETATM 5916 O O   . HOH G 4 .   ? -2.523  45.708  13.473  1.00 23.78 ? 524 HOH B O   1 
HETATM 5917 O O   . HOH G 4 .   ? 19.866  10.732  1.255   1.00 39.37 ? 525 HOH B O   1 
HETATM 5918 O O   . HOH G 4 .   ? 4.883   19.814  10.959  1.00 27.38 ? 526 HOH B O   1 
HETATM 5919 O O   . HOH G 4 .   ? -12.533 25.683  -6.067  1.00 29.83 ? 527 HOH B O   1 
HETATM 5920 O O   . HOH G 4 .   ? -5.256  34.948  -5.155  1.00 24.00 ? 528 HOH B O   1 
HETATM 5921 O O   . HOH G 4 .   ? 11.463  34.451  1.126   1.00 37.87 ? 529 HOH B O   1 
HETATM 5922 O O   . HOH G 4 .   ? -10.685 45.601  18.090  1.00 32.12 ? 530 HOH B O   1 
HETATM 5923 O O   . HOH G 4 .   ? -16.302 12.595  22.960  1.00 50.38 ? 531 HOH B O   1 
HETATM 5924 O O   . HOH G 4 .   ? -11.687 41.014  8.880   1.00 35.83 ? 532 HOH B O   1 
HETATM 5925 O O   . HOH G 4 .   ? 3.991   15.941  9.467   1.00 24.38 ? 533 HOH B O   1 
HETATM 5926 O O   . HOH G 4 .   ? -1.170  47.090  18.415  1.00 24.53 ? 534 HOH B O   1 
HETATM 5927 O O   . HOH G 4 .   ? 1.239   51.882  23.187  1.00 37.39 ? 535 HOH B O   1 
HETATM 5928 O O   . HOH G 4 .   ? 3.632   42.674  27.406  1.00 39.88 ? 536 HOH B O   1 
HETATM 5929 O O   . HOH G 4 .   ? 0.212   7.857   8.928   1.00 21.37 ? 537 HOH B O   1 
HETATM 5930 O O   . HOH G 4 .   ? 4.997   25.340  11.870  1.00 28.42 ? 538 HOH B O   1 
HETATM 5931 O O   . HOH G 4 .   ? 7.201   45.332  19.079  1.00 33.56 ? 539 HOH B O   1 
HETATM 5932 O O   . HOH G 4 .   ? -5.607  32.326  11.051  1.00 24.01 ? 540 HOH B O   1 
HETATM 5933 O O   . HOH G 4 .   ? 13.963  14.517  12.195  1.00 30.98 ? 541 HOH B O   1 
HETATM 5934 O O   . HOH G 4 .   ? -2.534  33.260  -8.853  1.00 30.33 ? 542 HOH B O   1 
HETATM 5935 O O   . HOH G 4 .   ? -8.884  11.303  17.277  1.00 37.71 ? 543 HOH B O   1 
HETATM 5936 O O   . HOH G 4 .   ? 14.611  15.729  14.535  1.00 37.27 ? 544 HOH B O   1 
HETATM 5937 O O   . HOH G 4 .   ? -21.963 18.701  14.023  1.00 35.30 ? 545 HOH B O   1 
HETATM 5938 O O   . HOH G 4 .   ? 4.363   46.647  27.295  1.00 45.74 ? 546 HOH B O   1 
HETATM 5939 O O   . HOH G 4 .   ? 14.678  6.058   5.720   1.00 34.06 ? 547 HOH B O   1 
HETATM 5940 O O   . HOH G 4 .   ? 0.488   39.654  15.369  1.00 24.04 ? 548 HOH B O   1 
HETATM 5941 O O   . HOH G 4 .   ? 4.292   37.863  9.502   1.00 24.91 ? 549 HOH B O   1 
HETATM 5942 O O   . HOH G 4 .   ? -21.476 12.562  7.943   1.00 38.59 ? 550 HOH B O   1 
HETATM 5943 O O   . HOH G 4 .   ? 9.588   19.842  -4.923  1.00 29.74 ? 551 HOH B O   1 
HETATM 5944 O O   . HOH G 4 .   ? 9.230   29.115  1.501   1.00 39.73 ? 552 HOH B O   1 
HETATM 5945 O O   . HOH G 4 .   ? 6.103   36.700  12.381  1.00 30.42 ? 553 HOH B O   1 
HETATM 5946 O O   . HOH G 4 .   ? -1.787  39.600  16.594  1.00 19.70 ? 554 HOH B O   1 
HETATM 5947 O O   . HOH G 4 .   ? -10.338 12.149  19.692  1.00 37.40 ? 555 HOH B O   1 
HETATM 5948 O O   . HOH G 4 .   ? 18.224  9.093   17.208  1.00 41.54 ? 556 HOH B O   1 
HETATM 5949 O O   . HOH G 4 .   ? 14.100  8.425   -2.317  1.00 43.12 ? 557 HOH B O   1 
HETATM 5950 O O   . HOH G 4 .   ? -2.844  31.042  9.023   1.00 26.58 ? 558 HOH B O   1 
HETATM 5951 O O   . HOH G 4 .   ? 3.843   29.225  22.144  1.00 40.64 ? 559 HOH B O   1 
HETATM 5952 O O   . HOH G 4 .   ? 11.265  26.617  4.024   1.00 33.28 ? 560 HOH B O   1 
HETATM 5953 O O   . HOH G 4 .   ? -2.939  44.532  27.985  1.00 35.08 ? 561 HOH B O   1 
HETATM 5954 O O   . HOH G 4 .   ? 4.183   0.719   4.788   1.00 31.94 ? 562 HOH B O   1 
HETATM 5955 O O   . HOH G 4 .   ? 12.149  6.195   18.251  1.00 40.94 ? 563 HOH B O   1 
HETATM 5956 O O   . HOH G 4 .   ? 5.781   37.617  31.946  1.00 41.51 ? 564 HOH B O   1 
HETATM 5957 O O   . HOH G 4 .   ? -8.103  48.042  3.549   1.00 21.84 ? 565 HOH B O   1 
HETATM 5958 O O   . HOH G 4 .   ? -0.087  51.196  12.606  1.00 25.00 ? 566 HOH B O   1 
HETATM 5959 O O   . HOH G 4 .   ? 0.678   23.445  -3.950  1.00 24.67 ? 567 HOH B O   1 
HETATM 5960 O O   . HOH G 4 .   ? -3.900  26.227  -9.267  1.00 35.05 ? 568 HOH B O   1 
HETATM 5961 O O   . HOH G 4 .   ? 4.443   41.937  22.199  1.00 33.48 ? 569 HOH B O   1 
HETATM 5962 O O   . HOH G 4 .   ? 8.637   39.878  28.606  1.00 49.65 ? 570 HOH B O   1 
HETATM 5963 O O   . HOH G 4 .   ? 13.286  21.080  11.997  1.00 35.51 ? 571 HOH B O   1 
HETATM 5964 O O   . HOH G 4 .   ? 6.777   13.770  13.692  1.00 23.93 ? 572 HOH B O   1 
HETATM 5965 O O   . HOH G 4 .   ? -4.950  48.716  23.397  1.00 32.29 ? 573 HOH B O   1 
HETATM 5966 O O   . HOH G 4 .   ? 4.198   50.036  21.803  1.00 35.48 ? 574 HOH B O   1 
HETATM 5967 O O   . HOH G 4 .   ? 7.275   2.915   4.783   1.00 23.71 ? 575 HOH B O   1 
HETATM 5968 O O   . HOH G 4 .   ? 10.557  37.724  1.298   1.00 35.90 ? 576 HOH B O   1 
HETATM 5969 O O   . HOH G 4 .   ? 17.418  8.817   7.353   1.00 39.33 ? 577 HOH B O   1 
HETATM 5970 O O   . HOH G 4 .   ? 2.624   53.041  18.732  1.00 24.84 ? 578 HOH B O   1 
HETATM 5971 O O   . HOH G 4 .   ? -0.149  42.154  14.223  1.00 23.28 ? 579 HOH B O   1 
HETATM 5972 O O   . HOH G 4 .   ? -0.585  53.017  24.551  1.00 43.97 ? 580 HOH B O   1 
HETATM 5973 O O   . HOH G 4 .   ? 1.325   30.026  21.361  1.00 33.53 ? 581 HOH B O   1 
HETATM 5974 O O   . HOH G 4 .   ? -5.353  50.831  17.596  1.00 33.07 ? 582 HOH B O   1 
HETATM 5975 O O   . HOH G 4 .   ? -12.794 42.180  13.352  1.00 33.47 ? 583 HOH B O   1 
HETATM 5976 O O   . HOH G 4 .   ? 8.579   31.417  25.331  1.00 46.85 ? 584 HOH B O   1 
HETATM 5977 O O   . HOH G 4 .   ? -21.333 25.124  15.595  1.00 43.16 ? 585 HOH B O   1 
HETATM 5978 O O   . HOH G 4 .   ? 5.750   21.568  26.606  1.00 44.00 ? 586 HOH B O   1 
HETATM 5979 O O   . HOH G 4 .   ? 2.297   38.906  7.509   1.00 21.28 ? 587 HOH B O   1 
HETATM 5980 O O   . HOH G 4 .   ? -0.162  0.872   6.102   1.00 25.82 ? 588 HOH B O   1 
HETATM 5981 O O   . HOH G 4 .   ? 2.491   33.442  7.441   1.00 25.47 ? 589 HOH B O   1 
HETATM 5982 O O   . HOH G 4 .   ? -4.320  33.189  -7.205  1.00 31.54 ? 590 HOH B O   1 
HETATM 5983 O O   . HOH G 4 .   ? -0.506  31.144  7.926   1.00 30.90 ? 591 HOH B O   1 
HETATM 5984 O O   . HOH G 4 .   ? 2.441   42.592  15.591  1.00 29.31 ? 592 HOH B O   1 
HETATM 5985 O O   . HOH G 4 .   ? -3.017  23.689  -8.282  1.00 36.39 ? 593 HOH B O   1 
HETATM 5986 O O   . HOH G 4 .   ? 2.903   2.713   0.248   1.00 27.95 ? 594 HOH B O   1 
HETATM 5987 O O   . HOH G 4 .   ? -11.629 23.231  8.704   1.00 31.61 ? 595 HOH B O   1 
HETATM 5988 O O   . HOH G 4 .   ? -5.883  33.118  35.266  1.00 45.00 ? 596 HOH B O   1 
HETATM 5989 O O   . HOH G 4 .   ? 1.981   44.157  13.673  1.00 30.10 ? 597 HOH B O   1 
HETATM 5990 O O   . HOH G 4 .   ? 7.805   37.786  14.087  1.00 33.35 ? 598 HOH B O   1 
HETATM 5991 O O   . HOH G 4 .   ? -5.012  22.222  27.207  1.00 44.78 ? 599 HOH B O   1 
HETATM 5992 O O   . HOH G 4 .   ? 3.241   46.474  4.466   1.00 27.85 ? 600 HOH B O   1 
HETATM 5993 O O   . HOH G 4 .   ? 9.441   21.867  17.537  1.00 38.01 ? 601 HOH B O   1 
HETATM 5994 O O   . HOH G 4 .   ? -13.495 14.274  -1.453  1.00 32.17 ? 602 HOH B O   1 
HETATM 5995 O O   . HOH G 4 .   ? 9.499   35.950  17.866  1.00 35.40 ? 603 HOH B O   1 
HETATM 5996 O O   . HOH G 4 .   ? 1.056   28.306  5.129   1.00 28.51 ? 604 HOH B O   1 
HETATM 5997 O O   . HOH G 4 .   ? -4.654  50.725  25.174  1.00 39.80 ? 605 HOH B O   1 
HETATM 5998 O O   . HOH G 4 .   ? -9.929  44.102  11.635  1.00 30.87 ? 606 HOH B O   1 
HETATM 5999 O O   . HOH G 4 .   ? 4.032   30.476  -11.713 1.00 35.10 ? 607 HOH B O   1 
HETATM 6000 O O   . HOH G 4 .   ? 9.878   28.853  4.514   1.00 41.12 ? 608 HOH B O   1 
HETATM 6001 O O   . HOH G 4 .   ? -4.132  3.422   13.855  1.00 40.48 ? 609 HOH B O   1 
HETATM 6002 O O   . HOH G 4 .   ? 5.106   30.021  6.057   1.00 39.24 ? 610 HOH B O   1 
HETATM 6003 O O   . HOH G 4 .   ? 4.024   45.482  24.868  1.00 34.52 ? 611 HOH B O   1 
HETATM 6004 O O   . HOH G 4 .   ? 10.796  24.672  6.659   1.00 36.77 ? 612 HOH B O   1 
HETATM 6005 O O   . HOH G 4 .   ? 9.920   29.833  20.929  1.00 45.61 ? 613 HOH B O   1 
HETATM 6006 O O   . HOH G 4 .   ? -1.538  22.874  -5.664  1.00 35.22 ? 614 HOH B O   1 
HETATM 6007 O O   . HOH G 4 .   ? 7.147   -3.009  10.236  1.00 33.93 ? 615 HOH B O   1 
HETATM 6008 O O   . HOH G 4 .   ? 3.468   0.942   2.247   1.00 40.59 ? 616 HOH B O   1 
HETATM 6009 O O   . HOH G 4 .   ? 8.100   29.934  23.103  1.00 43.48 ? 617 HOH B O   1 
HETATM 6010 O O   . HOH G 4 .   ? -9.349  44.316  7.464   1.00 29.42 ? 618 HOH B O   1 
HETATM 6011 O O   . HOH G 4 .   ? -10.781 41.217  11.590  1.00 28.51 ? 619 HOH B O   1 
HETATM 6012 O O   . HOH G 4 .   ? 6.866   23.006  17.448  1.00 36.32 ? 620 HOH B O   1 
HETATM 6013 O O   . HOH G 4 .   ? 4.801   42.911  24.858  1.00 33.95 ? 621 HOH B O   1 
HETATM 6014 O O   . HOH G 4 .   ? -20.377 12.354  10.668  1.00 42.07 ? 622 HOH B O   1 
HETATM 6015 O O   . HOH G 4 .   ? 1.567   0.221   4.626   1.00 39.77 ? 623 HOH B O   1 
HETATM 6016 O O   . HOH G 4 .   ? 10.847  3.392   21.258  1.00 53.54 ? 624 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASN A 2   ? 0.8583 0.9353 0.8848 0.1114  0.1606  -0.0374 3   ASN A N   
2    C CA  . ASN A 2   ? 0.8136 0.8730 0.8230 0.0991  0.1543  -0.0296 3   ASN A CA  
3    C C   . ASN A 2   ? 0.8275 0.8850 0.8151 0.0986  0.1704  -0.0220 3   ASN A C   
4    O O   . ASN A 2   ? 0.8320 0.8802 0.7906 0.1112  0.1764  -0.0261 3   ASN A O   
5    C CB  . ASN A 2   ? 0.8439 0.8745 0.8278 0.1015  0.1346  -0.0351 3   ASN A CB  
6    C CG  . ASN A 2   ? 0.8278 0.8556 0.8303 0.0929  0.1181  -0.0349 3   ASN A CG  
7    O OD1 . ASN A 2   ? 0.8355 0.8825 0.8688 0.0876  0.1194  -0.0328 3   ASN A OD1 
8    N ND2 . ASN A 2   ? 0.8151 0.8192 0.7991 0.0919  0.1022  -0.0368 3   ASN A ND2 
9    N N   . THR A 3   ? 0.8285 0.8932 0.8286 0.0847  0.1765  -0.0110 4   THR A N   
10   C CA  . THR A 3   ? 0.8637 0.9276 0.8467 0.0823  0.1926  -0.0012 4   THR A CA  
11   C C   . THR A 3   ? 0.9240 0.9581 0.8612 0.0870  0.1851  -0.0025 4   THR A C   
12   O O   . THR A 3   ? 0.8826 0.8978 0.8073 0.0888  0.1663  -0.0099 4   THR A O   
13   C CB  . THR A 3   ? 0.8363 0.9099 0.8441 0.0652  0.1958  0.0103  4   THR A CB  
14   O OG1 . THR A 3   ? 0.8019 0.8567 0.8014 0.0561  0.1771  0.0107  4   THR A OG1 
15   C CG2 . THR A 3   ? 0.8410 0.9424 0.8968 0.0604  0.1989  0.0098  4   THR A CG2 
16   N N   . PRO A 4   ? 0.8111 0.8398 0.7228 0.0896  0.1990  0.0047  5   PRO A N   
17   C CA  . PRO A 4   ? 0.7848 0.7840 0.6540 0.0930  0.1893  0.0036  5   PRO A CA  
18   C C   . PRO A 4   ? 0.7316 0.7166 0.6042 0.0794  0.1709  0.0060  5   PRO A C   
19   O O   . PRO A 4   ? 0.7251 0.6872 0.5743 0.0825  0.1546  -0.0003 5   PRO A O   
20   C CB  . PRO A 4   ? 0.8330 0.8334 0.6810 0.0955  0.2096  0.0143  5   PRO A CB  
21   C CG  . PRO A 4   ? 0.8226 0.8513 0.6932 0.1010  0.2310  0.0164  5   PRO A CG  
22   C CD  . PRO A 4   ? 0.8233 0.8720 0.7416 0.0918  0.2244  0.0135  5   PRO A CD  
23   N N   . LYS A 5   ? 0.7248 0.7231 0.6272 0.0647  0.1728  0.0145  6   LYS A N   
24   C CA  . LYS A 5   ? 0.6908 0.6783 0.5986 0.0527  0.1559  0.0161  6   LYS A CA  
25   C C   . LYS A 5   ? 0.6162 0.5998 0.5345 0.0538  0.1379  0.0066  6   LYS A C   
26   O O   . LYS A 5   ? 0.6073 0.5731 0.5127 0.0511  0.1222  0.0041  6   LYS A O   
27   C CB  . LYS A 5   ? 0.6075 0.6111 0.5468 0.0386  0.1613  0.0258  6   LYS A CB  
28   C CG  . LYS A 5   ? 0.6498 0.6437 0.5736 0.0318  0.1672  0.0366  6   LYS A CG  
29   C CD  . LYS A 5   ? 0.6482 0.6223 0.5584 0.0257  0.1488  0.0358  6   LYS A CD  
30   C CE  . LYS A 5   ? 0.6911 0.6512 0.5779 0.0223  0.1537  0.0452  6   LYS A CE  
31   N NZ  . LYS A 5   ? 0.7028 0.6781 0.6105 0.0145  0.1700  0.0568  6   LYS A NZ  
32   N N   . ASP A 6   ? 0.6531 0.6537 0.5963 0.0575  0.1401  0.0017  7   ASP A N   
33   C CA  . ASP A 6   ? 0.6338 0.6298 0.5854 0.0596  0.1240  -0.0064 7   ASP A CA  
34   C C   . ASP A 6   ? 0.6224 0.5934 0.5427 0.0676  0.1124  -0.0133 7   ASP A C   
35   O O   . ASP A 6   ? 0.5675 0.5250 0.4857 0.0631  0.0964  -0.0150 7   ASP A O   
36   C CB  . ASP A 6   ? 0.6935 0.7084 0.6688 0.0668  0.1292  -0.0120 7   ASP A CB  
37   C CG  . ASP A 6   ? 0.7272 0.7674 0.7393 0.0586  0.1375  -0.0067 7   ASP A CG  
38   O OD1 . ASP A 6   ? 0.6757 0.7170 0.7015 0.0472  0.1302  -0.0019 7   ASP A OD1 
39   O OD2 . ASP A 6   ? 0.7679 0.8275 0.7966 0.0642  0.1507  -0.0078 7   ASP A OD2 
40   N N   . GLN A 7   ? 0.6673 0.6320 0.5635 0.0800  0.1202  -0.0175 8   GLN A N   
41   C CA  . GLN A 7   ? 0.6379 0.5781 0.5050 0.0895  0.1077  -0.0260 8   GLN A CA  
42   C C   . GLN A 7   ? 0.5540 0.4740 0.4007 0.0830  0.0975  -0.0228 8   GLN A C   
43   O O   . GLN A 7   ? 0.5520 0.4549 0.3932 0.0819  0.0802  -0.0275 8   GLN A O   
44   C CB  . GLN A 7   ? 0.6743 0.6129 0.5179 0.1059  0.1190  -0.0317 8   GLN A CB  
45   C CG  . GLN A 7   ? 0.7293 0.6911 0.5938 0.1134  0.1321  -0.0345 8   GLN A CG  
46   C CD  . GLN A 7   ? 0.8211 0.7810 0.6600 0.1316  0.1431  -0.0410 8   GLN A CD  
47   O OE1 . GLN A 7   ? 0.8435 0.8229 0.6966 0.1399  0.1554  -0.0438 8   GLN A OE1 
48   N NE2 . GLN A 7   ? 0.8103 0.7468 0.6108 0.1389  0.1382  -0.0440 8   GLN A NE2 
49   N N   . GLU A 8   ? 0.5476 0.4693 0.3839 0.0787  0.1078  -0.0146 9   GLU A N   
50   C CA  . GLU A 8   ? 0.6299 0.5323 0.4452 0.0739  0.0982  -0.0120 9   GLU A CA  
51   C C   . GLU A 8   ? 0.5790 0.4800 0.4145 0.0610  0.0833  -0.0101 9   GLU A C   
52   O O   . GLU A 8   ? 0.5394 0.4224 0.3635 0.0601  0.0678  -0.0138 9   GLU A O   
53   C CB  . GLU A 8   ? 0.6236 0.5297 0.4277 0.0708  0.1130  -0.0018 9   GLU A CB  
54   C CG  . GLU A 8   ? 0.7261 0.6115 0.5060 0.0673  0.1032  0.0009  9   GLU A CG  
55   C CD  . GLU A 8   ? 0.8745 0.7658 0.6572 0.0577  0.1140  0.0136  9   GLU A CD  
56   O OE1 . GLU A 8   ? 0.8561 0.7676 0.6601 0.0532  0.1297  0.0208  9   GLU A OE1 
57   O OE2 . GLU A 8   ? 0.8383 0.7134 0.6031 0.0546  0.1058  0.0162  9   GLU A OE2 
58   N N   . ILE A 9   ? 0.5241 0.4446 0.3905 0.0515  0.0877  -0.0046 10  ILE A N   
59   C CA  . ILE A 9   ? 0.5295 0.4506 0.4138 0.0403  0.0755  -0.0020 10  ILE A CA  
60   C C   . ILE A 9   ? 0.5064 0.4208 0.3971 0.0426  0.0617  -0.0086 10  ILE A C   
61   O O   . ILE A 9   ? 0.4861 0.3900 0.3765 0.0373  0.0486  -0.0085 10  ILE A O   
62   C CB  . ILE A 9   ? 0.4833 0.4262 0.3971 0.0315  0.0833  0.0045  10  ILE A CB  
63   C CG1 . ILE A 9   ? 0.4889 0.4342 0.3968 0.0267  0.0942  0.0127  10  ILE A CG1 
64   C CG2 . ILE A 9   ? 0.4666 0.4118 0.3986 0.0231  0.0707  0.0055  10  ILE A CG2 
65   C CD1 . ILE A 9   ? 0.5350 0.4995 0.4731 0.0175  0.0999  0.0188  10  ILE A CD1 
66   N N   . LYS A 10  ? 0.4956 0.4158 0.3933 0.0505  0.0645  -0.0139 11  LYS A N   
67   C CA  . LYS A 10  ? 0.5321 0.4421 0.4326 0.0538  0.0512  -0.0198 11  LYS A CA  
68   C C   . LYS A 10  ? 0.5367 0.4224 0.4138 0.0569  0.0391  -0.0244 11  LYS A C   
69   O O   . LYS A 10  ? 0.5201 0.3958 0.4024 0.0517  0.0256  -0.0243 11  LYS A O   
70   C CB  . LYS A 10  ? 0.5401 0.4566 0.4459 0.0646  0.0559  -0.0261 11  LYS A CB  
71   C CG  . LYS A 10  ? 0.6134 0.5154 0.5196 0.0690  0.0415  -0.0321 11  LYS A CG  
72   C CD  . LYS A 10  ? 0.6339 0.5365 0.5371 0.0829  0.0446  -0.0406 11  LYS A CD  
73   C CE  . LYS A 10  ? 0.6691 0.5487 0.5628 0.0889  0.0287  -0.0477 11  LYS A CE  
74   N NZ  . LYS A 10  ? 0.6805 0.5557 0.5908 0.0793  0.0168  -0.0427 11  LYS A NZ  
75   N N   . LYS A 11  ? 0.5665 0.4425 0.4178 0.0657  0.0437  -0.0282 12  LYS A N   
76   C CA  . LYS A 11  ? 0.5617 0.4133 0.3896 0.0706  0.0304  -0.0344 12  LYS A CA  
77   C C   . LYS A 11  ? 0.5661 0.4106 0.3951 0.0596  0.0207  -0.0296 12  LYS A C   
78   O O   . LYS A 11  ? 0.5517 0.3818 0.3817 0.0574  0.0051  -0.0330 12  LYS A O   
79   C CB  . LYS A 11  ? 0.5585 0.4021 0.3554 0.0834  0.0383  -0.0390 12  LYS A CB  
80   C CG  . LYS A 11  ? 0.6888 0.5064 0.4613 0.0931  0.0230  -0.0492 12  LYS A CG  
81   C CD  . LYS A 11  ? 0.7767 0.5854 0.5139 0.1076  0.0308  -0.0538 12  LYS A CD  
82   C CE  . LYS A 11  ? 0.8312 0.6151 0.5463 0.1212  0.0147  -0.0673 12  LYS A CE  
83   N NZ  . LYS A 11  ? 0.9162 0.6820 0.5932 0.1313  0.0121  -0.0714 12  LYS A NZ  
84   N N   . LEU A 12  ? 0.5356 0.3904 0.3664 0.0525  0.0295  -0.0217 13  LEU A N   
85   C CA  . LEU A 12  ? 0.5290 0.3784 0.3615 0.0429  0.0205  -0.0176 13  LEU A CA  
86   C C   . LEU A 12  ? 0.5026 0.3577 0.3614 0.0337  0.0111  -0.0153 13  LEU A C   
87   O O   . LEU A 12  ? 0.4407 0.2859 0.3009 0.0292  -0.0017 -0.0159 13  LEU A O   
88   C CB  . LEU A 12  ? 0.5552 0.4151 0.3873 0.0372  0.0318  -0.0093 13  LEU A CB  
89   C CG  . LEU A 12  ? 0.5718 0.4241 0.3751 0.0449  0.0414  -0.0086 13  LEU A CG  
90   C CD1 . LEU A 12  ? 0.5470 0.4113 0.3564 0.0375  0.0536  0.0015  13  LEU A CD1 
91   C CD2 . LEU A 12  ? 0.6082 0.4368 0.3848 0.0499  0.0280  -0.0140 13  LEU A CD2 
92   N N   . VAL A 13  ? 0.4655 0.3373 0.3457 0.0312  0.0174  -0.0124 14  VAL A N   
93   C CA  . VAL A 13  ? 0.4569 0.3342 0.3591 0.0239  0.0098  -0.0092 14  VAL A CA  
94   C C   . VAL A 13  ? 0.5164 0.3790 0.4185 0.0273  -0.0021 -0.0142 14  VAL A C   
95   O O   . VAL A 13  ? 0.4550 0.3128 0.3669 0.0210  -0.0121 -0.0118 14  VAL A O   
96   C CB  . VAL A 13  ? 0.4317 0.3295 0.3544 0.0218  0.0186  -0.0053 14  VAL A CB  
97   C CG1 . VAL A 13  ? 0.4450 0.3468 0.3860 0.0166  0.0111  -0.0020 14  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.4351 0.3457 0.3618 0.0164  0.0275  0.0001  14  VAL A CG2 
99   N N   . ASP A 14  ? 0.4873 0.3422 0.3791 0.0374  -0.0012 -0.0210 15  ASP A N   
100  C CA  . ASP A 14  ? 0.5331 0.3705 0.4238 0.0412  -0.0142 -0.0266 15  ASP A CA  
101  C C   . ASP A 14  ? 0.5414 0.3605 0.4213 0.0394  -0.0272 -0.0296 15  ASP A C   
102  O O   . ASP A 14  ? 0.5876 0.3956 0.4774 0.0359  -0.0400 -0.0302 15  ASP A O   
103  C CB  . ASP A 14  ? 0.5250 0.3559 0.4033 0.0545  -0.0118 -0.0351 15  ASP A CB  
104  C CG  . ASP A 14  ? 0.5643 0.4106 0.4581 0.0571  -0.0036 -0.0337 15  ASP A CG  
105  O OD1 . ASP A 14  ? 0.5696 0.4281 0.4834 0.0492  -0.0026 -0.0267 15  ASP A OD1 
106  O OD2 . ASP A 14  ? 0.6323 0.4786 0.5177 0.0684  0.0016  -0.0403 15  ASP A OD2 
107  N N   . GLN A 15  ? 0.5314 0.3469 0.3919 0.0417  -0.0244 -0.0313 16  GLN A N   
108  C CA  . GLN A 15  ? 0.5606 0.3576 0.4084 0.0420  -0.0380 -0.0359 16  GLN A CA  
109  C C   . GLN A 15  ? 0.5185 0.3200 0.3837 0.0297  -0.0447 -0.0295 16  GLN A C   
110  O O   . GLN A 15  ? 0.5557 0.3434 0.4225 0.0278  -0.0593 -0.0331 16  GLN A O   
111  C CB  . GLN A 15  ? 0.5936 0.3842 0.4118 0.0500  -0.0327 -0.0392 16  GLN A CB  
112  C CG  . GLN A 15  ? 0.6712 0.4518 0.4659 0.0651  -0.0295 -0.0479 16  GLN A CG  
113  C CD  . GLN A 15  ? 0.7490 0.5268 0.5138 0.0728  -0.0199 -0.0481 16  GLN A CD  
114  O OE1 . GLN A 15  ? 0.7666 0.5430 0.5247 0.0677  -0.0207 -0.0437 16  GLN A OE1 
115  N NE2 . GLN A 15  ? 0.8299 0.6068 0.5759 0.0859  -0.0104 -0.0530 16  GLN A NE2 
116  N N   . ASN A 16  ? 0.4944 0.3152 0.3734 0.0219  -0.0350 -0.0209 17  ASN A N   
117  C CA  . ASN A 16  ? 0.4807 0.3071 0.3723 0.0121  -0.0399 -0.0156 17  ASN A CA  
118  C C   . ASN A 16  ? 0.4650 0.3056 0.3837 0.0038  -0.0391 -0.0083 17  ASN A C   
119  O O   . ASN A 16  ? 0.4732 0.3148 0.4052 -0.0032 -0.0466 -0.0053 17  ASN A O   
120  C CB  . ASN A 16  ? 0.5067 0.3412 0.3884 0.0107  -0.0311 -0.0120 17  ASN A CB  
121  C CG  . ASN A 16  ? 0.5451 0.3638 0.3982 0.0183  -0.0333 -0.0175 17  ASN A CG  
122  O OD1 . ASN A 16  ? 0.5186 0.3241 0.3645 0.0184  -0.0457 -0.0213 17  ASN A OD1 
123  N ND2 . ASN A 16  ? 0.5300 0.3498 0.3663 0.0256  -0.0214 -0.0182 17  ASN A ND2 
124  N N   . PHE A 17  ? 0.4269 0.2788 0.3539 0.0050  -0.0302 -0.0053 18  PHE A N   
125  C CA  . PHE A 17  ? 0.4220 0.2863 0.3709 -0.0010 -0.0293 0.0018  18  PHE A CA  
126  C C   . PHE A 17  ? 0.4522 0.3076 0.4094 0.0005  -0.0352 0.0015  18  PHE A C   
127  O O   . PHE A 17  ? 0.4433 0.3000 0.4164 -0.0055 -0.0400 0.0073  18  PHE A O   
128  C CB  . PHE A 17  ? 0.4170 0.2997 0.3713 -0.0007 -0.0175 0.0056  18  PHE A CB  
129  C CG  . PHE A 17  ? 0.3320 0.2253 0.2860 -0.0049 -0.0131 0.0085  18  PHE A CG  
130  C CD1 . PHE A 17  ? 0.3702 0.2613 0.3092 -0.0023 -0.0079 0.0060  18  PHE A CD1 
131  C CD2 . PHE A 17  ? 0.3979 0.3027 0.3660 -0.0109 -0.0143 0.0142  18  PHE A CD2 
132  C CE1 . PHE A 17  ? 0.3673 0.2662 0.3065 -0.0066 -0.0047 0.0092  18  PHE A CE1 
133  C CE2 . PHE A 17  ? 0.3477 0.2610 0.3155 -0.0141 -0.0116 0.0161  18  PHE A CE2 
134  C CZ  . PHE A 17  ? 0.3632 0.2727 0.3172 -0.0123 -0.0075 0.0136  18  PHE A CZ  
135  N N   . LYS A 18  ? 0.4588 0.3057 0.4059 0.0089  -0.0344 -0.0045 19  LYS A N   
136  C CA  . LYS A 18  ? 0.4924 0.3293 0.4470 0.0113  -0.0405 -0.0050 19  LYS A CA  
137  C C   . LYS A 18  ? 0.5189 0.3407 0.4824 0.0059  -0.0541 -0.0042 19  LYS A C   
138  O O   . LYS A 18  ? 0.5036 0.3245 0.4829 0.0019  -0.0570 0.0022  19  LYS A O   
139  C CB  . LYS A 18  ? 0.4792 0.3070 0.4186 0.0228  -0.0392 -0.0141 19  LYS A CB  
140  C CG  . LYS A 18  ? 0.5340 0.3516 0.4796 0.0271  -0.0450 -0.0155 19  LYS A CG  
141  C CD  . LYS A 18  ? 0.5444 0.3529 0.4729 0.0399  -0.0442 -0.0263 19  LYS A CD  
142  C CE  . LYS A 18  ? 0.5781 0.3723 0.5111 0.0455  -0.0527 -0.0294 19  LYS A CE  
143  N NZ  . LYS A 18  ? 0.6322 0.4116 0.5460 0.0586  -0.0567 -0.0420 19  LYS A NZ  
144  N N   . PRO A 19  ? 0.5068 0.3163 0.4621 0.0056  -0.0630 -0.0099 20  PRO A N   
145  C CA  . PRO A 19  ? 0.5007 0.2971 0.4701 -0.0005 -0.0770 -0.0092 20  PRO A CA  
146  C C   . PRO A 19  ? 0.5112 0.3214 0.5044 -0.0118 -0.0753 0.0024  20  PRO A C   
147  O O   . PRO A 19  ? 0.5140 0.3166 0.5252 -0.0177 -0.0838 0.0063  20  PRO A O   
148  C CB  . PRO A 19  ? 0.5301 0.3145 0.4844 0.0024  -0.0859 -0.0182 20  PRO A CB  
149  C CG  . PRO A 19  ? 0.5191 0.3022 0.4469 0.0133  -0.0781 -0.0253 20  PRO A CG  
150  C CD  . PRO A 19  ? 0.5239 0.3284 0.4561 0.0121  -0.0619 -0.0179 20  PRO A CD  
151  N N   . LEU A 20  ? 0.4654 0.2957 0.4599 -0.0148 -0.0645 0.0081  21  LEU A N   
152  C CA  . LEU A 20  ? 0.4871 0.3320 0.5021 -0.0236 -0.0617 0.0187  21  LEU A CA  
153  C C   . LEU A 20  ? 0.4784 0.3247 0.5072 -0.0254 -0.0592 0.0275  21  LEU A C   
154  O O   . LEU A 20  ? 0.4354 0.2879 0.4829 -0.0327 -0.0596 0.0368  21  LEU A O   
155  C CB  . LEU A 20  ? 0.4345 0.2994 0.4456 -0.0241 -0.0511 0.0217  21  LEU A CB  
156  C CG  . LEU A 20  ? 0.4393 0.3026 0.4375 -0.0232 -0.0533 0.0152  21  LEU A CG  
157  C CD1 . LEU A 20  ? 0.3769 0.2584 0.3726 -0.0236 -0.0433 0.0185  21  LEU A CD1 
158  C CD2 . LEU A 20  ? 0.4607 0.3184 0.4698 -0.0288 -0.0644 0.0145  21  LEU A CD2 
159  N N   . LEU A 21  ? 0.4857 0.3268 0.5055 -0.0184 -0.0563 0.0251  22  LEU A N   
160  C CA  . LEU A 21  ? 0.5077 0.3487 0.5378 -0.0188 -0.0543 0.0336  22  LEU A CA  
161  C C   . LEU A 21  ? 0.4942 0.3191 0.5397 -0.0246 -0.0647 0.0378  22  LEU A C   
162  O O   . LEU A 21  ? 0.4437 0.2737 0.5053 -0.0308 -0.0624 0.0499  22  LEU A O   
163  C CB  . LEU A 21  ? 0.4426 0.2793 0.4603 -0.0091 -0.0514 0.0284  22  LEU A CB  
164  C CG  . LEU A 21  ? 0.5554 0.4093 0.5636 -0.0038 -0.0405 0.0260  22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.5575 0.4054 0.5569 0.0060  -0.0396 0.0195  22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.4780 0.3500 0.4954 -0.0071 -0.0332 0.0361  22  LEU A CD2 
167  N N   . GLU A 22  ? 0.5100 0.3145 0.5509 -0.0221 -0.0764 0.0281  23  GLU A N   
168  C CA  . GLU A 22  ? 0.5394 0.3269 0.5978 -0.0281 -0.0885 0.0312  23  GLU A CA  
169  C C   . GLU A 22  ? 0.5466 0.3405 0.6232 -0.0384 -0.0924 0.0354  23  GLU A C   
170  O O   . GLU A 22  ? 0.5385 0.3294 0.6385 -0.0470 -0.0963 0.0448  23  GLU A O   
171  C CB  . GLU A 22  ? 0.6176 0.3802 0.6651 -0.0209 -0.1020 0.0178  23  GLU A CB  
172  C CG  . GLU A 22  ? 0.7526 0.4943 0.8195 -0.0264 -0.1162 0.0203  23  GLU A CG  
173  C CD  . GLU A 22  ? 0.9001 0.6160 0.9553 -0.0182 -0.1321 0.0047  23  GLU A CD  
174  O OE1 . GLU A 22  ? 0.9384 0.6366 1.0102 -0.0234 -0.1474 0.0032  23  GLU A OE1 
175  O OE2 . GLU A 22  ? 0.9623 0.6759 0.9921 -0.0061 -0.1293 -0.0061 23  GLU A OE2 
176  N N   . LYS A 23  ? 0.5429 0.3462 0.6105 -0.0376 -0.0911 0.0290  24  LYS A N   
177  C CA  . LYS A 23  ? 0.5070 0.3161 0.5920 -0.0460 -0.0964 0.0310  24  LYS A CA  
178  C C   . LYS A 23  ? 0.4954 0.3251 0.6013 -0.0543 -0.0863 0.0462  24  LYS A C   
179  O O   . LYS A 23  ? 0.5038 0.3357 0.6346 -0.0632 -0.0910 0.0523  24  LYS A O   
180  C CB  . LYS A 23  ? 0.5032 0.3175 0.5711 -0.0422 -0.0966 0.0217  24  LYS A CB  
181  C CG  . LYS A 23  ? 0.5454 0.3613 0.6297 -0.0489 -0.1062 0.0203  24  LYS A CG  
182  C CD  . LYS A 23  ? 0.6114 0.4319 0.6771 -0.0446 -0.1062 0.0122  24  LYS A CD  
183  C CE  . LYS A 23  ? 0.5905 0.4125 0.6739 -0.0505 -0.1172 0.0102  24  LYS A CE  
184  N NZ  . LYS A 23  ? 0.5685 0.3916 0.6325 -0.0456 -0.1192 0.0022  24  LYS A NZ  
185  N N   . TYR A 24  ? 0.4992 0.3444 0.5961 -0.0510 -0.0724 0.0524  25  TYR A N   
186  C CA  . TYR A 24  ? 0.4635 0.3292 0.5751 -0.0562 -0.0619 0.0660  25  TYR A CA  
187  C C   . TYR A 24  ? 0.4634 0.3296 0.5761 -0.0547 -0.0543 0.0770  25  TYR A C   
188  O O   . TYR A 24  ? 0.4730 0.3567 0.5908 -0.0559 -0.0438 0.0879  25  TYR A O   
189  C CB  . TYR A 24  ? 0.4769 0.3626 0.5775 -0.0531 -0.0534 0.0637  25  TYR A CB  
190  C CG  . TYR A 24  ? 0.5053 0.3919 0.6079 -0.0556 -0.0606 0.0558  25  TYR A CG  
191  C CD1 . TYR A 24  ? 0.4680 0.3630 0.5942 -0.0634 -0.0637 0.0608  25  TYR A CD1 
192  C CD2 . TYR A 24  ? 0.4636 0.3425 0.5450 -0.0498 -0.0645 0.0436  25  TYR A CD2 
193  C CE1 . TYR A 24  ? 0.5092 0.4044 0.6377 -0.0648 -0.0719 0.0529  25  TYR A CE1 
194  C CE2 . TYR A 24  ? 0.5229 0.4006 0.6038 -0.0511 -0.0720 0.0366  25  TYR A CE2 
195  C CZ  . TYR A 24  ? 0.5261 0.4115 0.6304 -0.0584 -0.0764 0.0408  25  TYR A CZ  
196  O OH  . TYR A 24  ? 0.5207 0.4046 0.6247 -0.0588 -0.0852 0.0332  25  TYR A OH  
197  N N   . ASP A 25  ? 0.4951 0.3418 0.6019 -0.0510 -0.0600 0.0742  26  ASP A N   
198  C CA  . ASP A 25  ? 0.4682 0.3112 0.5743 -0.0485 -0.0550 0.0840  26  ASP A CA  
199  C C   . ASP A 25  ? 0.4366 0.2982 0.5289 -0.0419 -0.0424 0.0874  26  ASP A C   
200  O O   . ASP A 25  ? 0.4152 0.2857 0.5119 -0.0424 -0.0344 0.1003  26  ASP A O   
201  C CB  . ASP A 25  ? 0.4493 0.2899 0.5798 -0.0580 -0.0550 0.0994  26  ASP A CB  
202  C CG  . ASP A 25  ? 0.5739 0.4018 0.7028 -0.0554 -0.0538 0.1086  26  ASP A CG  
203  O OD1 . ASP A 25  ? 0.5793 0.3951 0.6910 -0.0465 -0.0574 0.1001  26  ASP A OD1 
204  O OD2 . ASP A 25  ? 0.5621 0.3924 0.7069 -0.0617 -0.0489 0.1249  26  ASP A OD2 
205  N N   . VAL A 26  ? 0.4156 0.2819 0.4905 -0.0349 -0.0409 0.0758  27  VAL A N   
206  C CA  . VAL A 26  ? 0.4266 0.3097 0.4899 -0.0284 -0.0313 0.0762  27  VAL A CA  
207  C C   . VAL A 26  ? 0.3837 0.2578 0.4365 -0.0199 -0.0314 0.0740  27  VAL A C   
208  O O   . VAL A 26  ? 0.4098 0.2708 0.4552 -0.0158 -0.0371 0.0638  27  VAL A O   
209  C CB  . VAL A 26  ? 0.4167 0.3098 0.4702 -0.0264 -0.0297 0.0657  27  VAL A CB  
210  C CG1 . VAL A 26  ? 0.3698 0.2778 0.4138 -0.0195 -0.0217 0.0650  27  VAL A CG1 
211  C CG2 . VAL A 26  ? 0.4593 0.3615 0.5228 -0.0336 -0.0303 0.0675  27  VAL A CG2 
212  N N   . PRO A 27  ? 0.4236 0.3041 0.4744 -0.0159 -0.0257 0.0828  28  PRO A N   
213  C CA  . PRO A 27  ? 0.3963 0.2673 0.4381 -0.0070 -0.0274 0.0801  28  PRO A CA  
214  C C   . PRO A 27  ? 0.3733 0.2507 0.4041 0.0008  -0.0262 0.0669  28  PRO A C   
215  O O   . PRO A 27  ? 0.3810 0.2466 0.4066 0.0068  -0.0304 0.0596  28  PRO A O   
216  C CB  . PRO A 27  ? 0.3909 0.2696 0.4317 -0.0039 -0.0214 0.0928  28  PRO A CB  
217  C CG  . PRO A 27  ? 0.4277 0.3138 0.4800 -0.0128 -0.0174 0.1046  28  PRO A CG  
218  C CD  . PRO A 27  ? 0.4164 0.3104 0.4734 -0.0185 -0.0185 0.0962  28  PRO A CD  
219  N N   . GLY A 28  ? 0.3804 0.2763 0.4086 0.0014  -0.0204 0.0640  29  GLY A N   
220  C CA  . GLY A 28  ? 0.3638 0.2676 0.3851 0.0082  -0.0180 0.0535  29  GLY A CA  
221  C C   . GLY A 28  ? 0.3322 0.2489 0.3527 0.0048  -0.0144 0.0485  29  GLY A C   
222  O O   . GLY A 28  ? 0.3270 0.2521 0.3515 -0.0007 -0.0127 0.0536  29  GLY A O   
223  N N   . MET A 29  ? 0.2925 0.2113 0.3081 0.0084  -0.0128 0.0389  30  MET A N   
224  C CA  . MET A 29  ? 0.3053 0.2337 0.3192 0.0053  -0.0094 0.0345  30  MET A CA  
225  C C   . MET A 29  ? 0.3019 0.2386 0.3142 0.0109  -0.0049 0.0271  30  MET A C   
226  O O   . MET A 29  ? 0.3210 0.2519 0.3311 0.0168  -0.0050 0.0222  30  MET A O   
227  C CB  . MET A 29  ? 0.3251 0.2416 0.3345 0.0004  -0.0130 0.0314  30  MET A CB  
228  C CG  . MET A 29  ? 0.3500 0.2731 0.3547 -0.0022 -0.0100 0.0272  30  MET A CG  
229  S SD  . MET A 29  ? 0.4444 0.3506 0.4390 -0.0046 -0.0156 0.0218  30  MET A SD  
230  C CE  . MET A 29  ? 0.4055 0.3094 0.4105 -0.0128 -0.0223 0.0286  30  MET A CE  
231  N N   . ALA A 30  ? 0.3266 0.2772 0.3418 0.0092  -0.0011 0.0262  31  ALA A N   
232  C CA  . ALA A 30  ? 0.2936 0.2530 0.3107 0.0122  0.0040  0.0201  31  ALA A CA  
233  C C   . ALA A 30  ? 0.3078 0.2687 0.3210 0.0065  0.0067  0.0189  31  ALA A C   
234  O O   . ALA A 30  ? 0.3033 0.2684 0.3180 0.0019  0.0049  0.0224  31  ALA A O   
235  C CB  . ALA A 30  ? 0.2993 0.2736 0.3263 0.0161  0.0047  0.0200  31  ALA A CB  
236  N N   . VAL A 31  ? 0.2695 0.2263 0.2764 0.0077  0.0109  0.0143  32  VAL A N   
237  C CA  . VAL A 31  ? 0.3137 0.2701 0.3144 0.0033  0.0140  0.0139  32  VAL A CA  
238  C C   . VAL A 31  ? 0.2735 0.2393 0.2783 0.0054  0.0226  0.0111  32  VAL A C   
239  O O   . VAL A 31  ? 0.2932 0.2584 0.2969 0.0111  0.0267  0.0074  32  VAL A O   
240  C CB  . VAL A 31  ? 0.3441 0.2836 0.3293 0.0027  0.0110  0.0121  32  VAL A CB  
241  C CG1 . VAL A 31  ? 0.3454 0.2832 0.3215 -0.0009 0.0138  0.0122  32  VAL A CG1 
242  C CG2 . VAL A 31  ? 0.3326 0.2642 0.3190 -0.0006 0.0024  0.0153  32  VAL A CG2 
243  N N   . GLY A 32  ? 0.2797 0.2540 0.2900 0.0009  0.0253  0.0130  33  GLY A N   
244  C CA  . GLY A 32  ? 0.2779 0.2621 0.2962 0.0013  0.0339  0.0120  33  GLY A CA  
245  C C   . GLY A 32  ? 0.2911 0.2724 0.3026 -0.0041 0.0380  0.0148  33  GLY A C   
246  O O   . GLY A 32  ? 0.2709 0.2466 0.2766 -0.0085 0.0325  0.0172  33  GLY A O   
247  N N   . VAL A 33  ? 0.2710 0.2559 0.2830 -0.0031 0.0481  0.0150  34  VAL A N   
248  C CA  . VAL A 33  ? 0.2993 0.2816 0.3054 -0.0079 0.0541  0.0192  34  VAL A CA  
249  C C   . VAL A 33  ? 0.3079 0.3062 0.3362 -0.0103 0.0622  0.0210  34  VAL A C   
250  O O   . VAL A 33  ? 0.3154 0.3244 0.3559 -0.0059 0.0680  0.0183  34  VAL A O   
251  C CB  . VAL A 33  ? 0.3485 0.3175 0.3302 -0.0039 0.0601  0.0192  34  VAL A CB  
252  C CG1 . VAL A 33  ? 0.3314 0.3000 0.3079 -0.0073 0.0701  0.0249  34  VAL A CG1 
253  C CG2 . VAL A 33  ? 0.3460 0.2981 0.3084 -0.0033 0.0496  0.0175  34  VAL A CG2 
254  N N   . ILE A 34  ? 0.2695 0.2699 0.3056 -0.0171 0.0615  0.0251  35  ILE A N   
255  C CA  . ILE A 34  ? 0.2806 0.2942 0.3395 -0.0211 0.0689  0.0278  35  ILE A CA  
256  C C   . ILE A 34  ? 0.3130 0.3181 0.3594 -0.0255 0.0780  0.0351  35  ILE A C   
257  O O   . ILE A 34  ? 0.3032 0.2943 0.3318 -0.0280 0.0725  0.0375  35  ILE A O   
258  C CB  . ILE A 34  ? 0.2703 0.2926 0.3517 -0.0250 0.0589  0.0263  35  ILE A CB  
259  C CG1 . ILE A 34  ? 0.3299 0.3645 0.4382 -0.0304 0.0648  0.0291  35  ILE A CG1 
260  C CG2 . ILE A 34  ? 0.2459 0.2568 0.3144 -0.0281 0.0484  0.0274  35  ILE A CG2 
261  C CD1 . ILE A 34  ? 0.3640 0.4165 0.4992 -0.0269 0.0665  0.0243  35  ILE A CD1 
262  N N   . GLN A 35  ? 0.3330 0.3462 0.3871 -0.0254 0.0922  0.0387  36  GLN A N   
263  C CA  . GLN A 35  ? 0.3374 0.3428 0.3788 -0.0290 0.1031  0.0474  36  GLN A CA  
264  C C   . GLN A 35  ? 0.3732 0.3954 0.4421 -0.0330 0.1166  0.0527  36  GLN A C   
265  O O   . GLN A 35  ? 0.3216 0.3577 0.4024 -0.0280 0.1251  0.0497  36  GLN A O   
266  C CB  . GLN A 35  ? 0.3972 0.3892 0.4042 -0.0214 0.1097  0.0475  36  GLN A CB  
267  C CG  . GLN A 35  ? 0.4392 0.4220 0.4287 -0.0233 0.1220  0.0573  36  GLN A CG  
268  C CD  . GLN A 35  ? 0.5451 0.5170 0.5008 -0.0133 0.1304  0.0567  36  GLN A CD  
269  O OE1 . GLN A 35  ? 0.5837 0.5633 0.5397 -0.0053 0.1359  0.0513  36  GLN A OE1 
270  N NE2 . GLN A 35  ? 0.5863 0.5392 0.5119 -0.0125 0.1307  0.0617  36  GLN A NE2 
271  N N   . ASN A 36  ? 0.3476 0.3687 0.4283 -0.0421 0.1184  0.0604  37  ASN A N   
272  C CA  . ASN A 36  ? 0.3905 0.4268 0.5003 -0.0478 0.1318  0.0674  37  ASN A CA  
273  C C   . ASN A 36  ? 0.3716 0.4304 0.5174 -0.0463 0.1301  0.0601  37  ASN A C   
274  O O   . ASN A 36  ? 0.3747 0.4493 0.5369 -0.0443 0.1441  0.0617  37  ASN A O   
275  C CB  . ASN A 36  ? 0.4525 0.4873 0.5441 -0.0446 0.1522  0.0757  37  ASN A CB  
276  C CG  . ASN A 36  ? 0.4898 0.5014 0.5455 -0.0456 0.1538  0.0837  37  ASN A CG  
277  O OD1 . ASN A 36  ? 0.5784 0.5781 0.5988 -0.0372 0.1584  0.0832  37  ASN A OD1 
278  N ND2 . ASN A 36  ? 0.4766 0.4807 0.5408 -0.0552 0.1487  0.0904  37  ASN A ND2 
279  N N   . ASN A 37  ? 0.3616 0.4219 0.5188 -0.0459 0.1127  0.0518  38  ASN A N   
280  C CA  . ASN A 37  ? 0.3935 0.4723 0.5830 -0.0436 0.1066  0.0437  38  ASN A CA  
281  C C   . ASN A 37  ? 0.3786 0.4648 0.5620 -0.0331 0.1103  0.0369  38  ASN A C   
282  O O   . ASN A 37  ? 0.3892 0.4922 0.6001 -0.0301 0.1081  0.0309  38  ASN A O   
283  C CB  . ASN A 37  ? 0.3806 0.4770 0.6114 -0.0509 0.1139  0.0478  38  ASN A CB  
284  C CG  . ASN A 37  ? 0.4354 0.5231 0.6725 -0.0621 0.1142  0.0572  38  ASN A CG  
285  O OD1 . ASN A 37  ? 0.4671 0.5423 0.6971 -0.0648 0.0995  0.0554  38  ASN A OD1 
286  N ND2 . ASN A 37  ? 0.5246 0.6187 0.7750 -0.0682 0.1314  0.0678  38  ASN A ND2 
287  N N   . LYS A 38  ? 0.3714 0.4448 0.5203 -0.0268 0.1146  0.0369  39  LYS A N   
288  C CA  . LYS A 38  ? 0.3383 0.4154 0.4795 -0.0162 0.1159  0.0297  39  LYS A CA  
289  C C   . LYS A 38  ? 0.3455 0.4069 0.4622 -0.0117 0.1015  0.0242  39  LYS A C   
290  O O   . LYS A 38  ? 0.3341 0.3785 0.4254 -0.0138 0.0978  0.0273  39  LYS A O   
291  C CB  . LYS A 38  ? 0.3703 0.4463 0.4935 -0.0107 0.1330  0.0330  39  LYS A CB  
292  C CG  . LYS A 38  ? 0.4523 0.5470 0.6011 -0.0139 0.1506  0.0392  39  LYS A CG  
293  C CD  . LYS A 38  ? 0.4798 0.5749 0.6081 -0.0052 0.1676  0.0409  39  LYS A CD  
294  C CE  . LYS A 38  ? 0.5563 0.6691 0.7065 -0.0092 0.1882  0.0502  39  LYS A CE  
295  N NZ  . LYS A 38  ? 0.6125 0.7214 0.7329 0.0002  0.2056  0.0535  39  LYS A NZ  
296  N N   . LYS A 39  ? 0.3054 0.3727 0.4306 -0.0052 0.0935  0.0167  40  LYS A N   
297  C CA  . LYS A 39  ? 0.3064 0.3607 0.4129 -0.0012 0.0806  0.0126  40  LYS A CA  
298  C C   . LYS A 39  ? 0.3171 0.3626 0.4021 0.0074  0.0841  0.0094  40  LYS A C   
299  O O   . LYS A 39  ? 0.3140 0.3691 0.4068 0.0134  0.0927  0.0066  40  LYS A O   
300  C CB  . LYS A 39  ? 0.2687 0.3321 0.3947 0.0014  0.0688  0.0072  40  LYS A CB  
301  C CG  . LYS A 39  ? 0.2971 0.3676 0.4433 -0.0050 0.0615  0.0081  40  LYS A CG  
302  C CD  . LYS A 39  ? 0.3173 0.3934 0.4744 0.0007  0.0486  0.0019  40  LYS A CD  
303  C CE  . LYS A 39  ? 0.3224 0.4058 0.4997 -0.0033 0.0394  0.0006  40  LYS A CE  
304  N NZ  . LYS A 39  ? 0.2835 0.3700 0.4653 0.0041  0.0260  -0.0054 40  LYS A NZ  
305  N N   . TYR A 40  ? 0.2870 0.3145 0.3468 0.0082  0.0767  0.0093  41  TYR A N   
306  C CA  . TYR A 40  ? 0.3395 0.3553 0.3793 0.0164  0.0758  0.0051  41  TYR A CA  
307  C C   . TYR A 40  ? 0.3370 0.3427 0.3711 0.0169  0.0617  0.0032  41  TYR A C   
308  O O   . TYR A 40  ? 0.3280 0.3251 0.3539 0.0112  0.0550  0.0065  41  TYR A O   
309  C CB  . TYR A 40  ? 0.3406 0.3418 0.3531 0.0171  0.0816  0.0073  41  TYR A CB  
310  C CG  . TYR A 40  ? 0.3718 0.3817 0.3868 0.0159  0.0972  0.0118  41  TYR A CG  
311  C CD1 . TYR A 40  ? 0.3689 0.3807 0.3891 0.0068  0.1003  0.0190  41  TYR A CD1 
312  C CD2 . TYR A 40  ? 0.3949 0.4113 0.4076 0.0243  0.1093  0.0094  41  TYR A CD2 
313  C CE1 . TYR A 40  ? 0.4033 0.4223 0.4265 0.0049  0.1155  0.0251  41  TYR A CE1 
314  C CE2 . TYR A 40  ? 0.4564 0.4820 0.4718 0.0232  0.1256  0.0152  41  TYR A CE2 
315  C CZ  . TYR A 40  ? 0.4415 0.4681 0.4627 0.0129  0.1289  0.0237  41  TYR A CZ  
316  O OH  . TYR A 40  ? 0.4414 0.4765 0.4662 0.0110  0.1459  0.0312  41  TYR A OH  
317  N N   . GLU A 41  ? 0.3055 0.3126 0.3449 0.0238  0.0575  -0.0014 42  GLU A N   
318  C CA  . GLU A 41  ? 0.3372 0.3376 0.3757 0.0243  0.0454  -0.0015 42  GLU A CA  
319  C C   . GLU A 41  ? 0.3410 0.3256 0.3640 0.0306  0.0409  -0.0046 42  GLU A C   
320  O O   . GLU A 41  ? 0.3514 0.3371 0.3747 0.0386  0.0445  -0.0096 42  GLU A O   
321  C CB  . GLU A 41  ? 0.3054 0.3203 0.3657 0.0271  0.0420  -0.0034 42  GLU A CB  
322  C CG  . GLU A 41  ? 0.3027 0.3314 0.3801 0.0209  0.0431  -0.0012 42  GLU A CG  
323  C CD  . GLU A 41  ? 0.4206 0.4650 0.5215 0.0252  0.0401  -0.0051 42  GLU A CD  
324  O OE1 . GLU A 41  ? 0.4358 0.4795 0.5378 0.0332  0.0361  -0.0088 42  GLU A OE1 
325  O OE2 . GLU A 41  ? 0.4249 0.4812 0.5434 0.0207  0.0405  -0.0047 42  GLU A OE2 
326  N N   . MET A 42  ? 0.3123 0.2824 0.3234 0.0271  0.0327  -0.0019 43  MET A N   
327  C CA  . MET A 42  ? 0.3628 0.3157 0.3617 0.0315  0.0260  -0.0043 43  MET A CA  
328  C C   . MET A 42  ? 0.3421 0.2908 0.3463 0.0297  0.0167  -0.0002 43  MET A C   
329  O O   . MET A 42  ? 0.3350 0.2855 0.3412 0.0229  0.0138  0.0051  43  MET A O   
330  C CB  . MET A 42  ? 0.3748 0.3121 0.3549 0.0290  0.0242  -0.0045 43  MET A CB  
331  C CG  . MET A 42  ? 0.4440 0.3781 0.4106 0.0352  0.0319  -0.0096 43  MET A CG  
332  S SD  . MET A 42  ? 0.6172 0.5697 0.5899 0.0330  0.0469  -0.0071 43  MET A SD  
333  C CE  . MET A 42  ? 0.4226 0.3762 0.3977 0.0211  0.0435  0.0001  43  MET A CE  
334  N N   . TYR A 43  ? 0.3314 0.2740 0.3371 0.0363  0.0123  -0.0024 44  TYR A N   
335  C CA  . TYR A 43  ? 0.3418 0.2793 0.3513 0.0355  0.0045  0.0028  44  TYR A CA  
336  C C   . TYR A 43  ? 0.3599 0.2764 0.3606 0.0371  -0.0029 0.0025  44  TYR A C   
337  O O   . TYR A 43  ? 0.3877 0.2958 0.3822 0.0440  -0.0033 -0.0043 44  TYR A O   
338  C CB  . TYR A 43  ? 0.3191 0.2673 0.3399 0.0423  0.0043  0.0017  44  TYR A CB  
339  C CG  . TYR A 43  ? 0.3177 0.2861 0.3503 0.0407  0.0097  0.0009  44  TYR A CG  
340  C CD1 . TYR A 43  ? 0.2995 0.2748 0.3356 0.0351  0.0081  0.0062  44  TYR A CD1 
341  C CD2 . TYR A 43  ? 0.3318 0.3126 0.3737 0.0450  0.0164  -0.0053 44  TYR A CD2 
342  C CE1 . TYR A 43  ? 0.2898 0.2815 0.3376 0.0338  0.0111  0.0047  44  TYR A CE1 
343  C CE2 . TYR A 43  ? 0.2886 0.2874 0.3450 0.0424  0.0203  -0.0057 44  TYR A CE2 
344  C CZ  . TYR A 43  ? 0.3047 0.3076 0.3637 0.0368  0.0167  -0.0011 44  TYR A CZ  
345  O OH  . TYR A 43  ? 0.2826 0.3012 0.3566 0.0344  0.0186  -0.0022 44  TYR A OH  
346  N N   . TYR A 44  ? 0.3257 0.2339 0.3268 0.0310  -0.0088 0.0098  45  TYR A N   
347  C CA  . TYR A 44  ? 0.3502 0.2378 0.3471 0.0305  -0.0171 0.0109  45  TYR A CA  
348  C C   . TYR A 44  ? 0.3447 0.2289 0.3487 0.0279  -0.0214 0.0207  45  TYR A C   
349  O O   . TYR A 44  ? 0.3420 0.2378 0.3509 0.0232  -0.0185 0.0278  45  TYR A O   
350  C CB  . TYR A 44  ? 0.4115 0.2897 0.4028 0.0236  -0.0204 0.0106  45  TYR A CB  
351  C CG  . TYR A 44  ? 0.4130 0.2931 0.3938 0.0254  -0.0160 0.0031  45  TYR A CG  
352  C CD1 . TYR A 44  ? 0.4726 0.3406 0.4419 0.0331  -0.0177 -0.0058 45  TYR A CD1 
353  C CD2 . TYR A 44  ? 0.4433 0.3360 0.4240 0.0200  -0.0102 0.0051  45  TYR A CD2 
354  C CE1 . TYR A 44  ? 0.4671 0.3363 0.4236 0.0357  -0.0125 -0.0115 45  TYR A CE1 
355  C CE2 . TYR A 44  ? 0.4714 0.3641 0.4407 0.0215  -0.0056 -0.0001 45  TYR A CE2 
356  C CZ  . TYR A 44  ? 0.4822 0.3636 0.4388 0.0295  -0.0062 -0.0079 45  TYR A CZ  
357  O OH  . TYR A 44  ? 0.4594 0.3406 0.4019 0.0320  -0.0004 -0.0120 45  TYR A OH  
358  N N   . GLY A 45  ? 0.3754 0.2429 0.3790 0.0314  -0.0282 0.0215  46  GLY A N   
359  C CA  . GLY A 45  ? 0.4214 0.2815 0.4306 0.0271  -0.0321 0.0329  46  GLY A CA  
360  C C   . GLY A 45  ? 0.3951 0.2656 0.4066 0.0315  -0.0291 0.0393  46  GLY A C   
361  O O   . GLY A 45  ? 0.3474 0.2268 0.3578 0.0398  -0.0269 0.0334  46  GLY A O   
362  N N   . LEU A 46  ? 0.3620 0.2313 0.3770 0.0264  -0.0291 0.0517  47  LEU A N   
363  C CA  . LEU A 46  ? 0.3792 0.2519 0.3927 0.0318  -0.0281 0.0596  47  LEU A CA  
364  C C   . LEU A 46  ? 0.4085 0.3014 0.4222 0.0304  -0.0217 0.0644  47  LEU A C   
365  O O   . LEU A 46  ? 0.3756 0.2743 0.3929 0.0222  -0.0187 0.0695  47  LEU A O   
366  C CB  . LEU A 46  ? 0.4009 0.2554 0.4162 0.0291  -0.0323 0.0718  47  LEU A CB  
367  C CG  . LEU A 46  ? 0.4005 0.2321 0.4159 0.0316  -0.0410 0.0671  47  LEU A CG  
368  C CD1 . LEU A 46  ? 0.4340 0.2464 0.4536 0.0275  -0.0455 0.0810  47  LEU A CD1 
369  C CD2 . LEU A 46  ? 0.4166 0.2480 0.4259 0.0445  -0.0433 0.0568  47  LEU A CD2 
370  N N   . GLN A 47  ? 0.3437 0.2469 0.3541 0.0393  -0.0207 0.0618  48  GLN A N   
371  C CA  . GLN A 47  ? 0.3832 0.3023 0.3914 0.0412  -0.0170 0.0664  48  GLN A CA  
372  C C   . GLN A 47  ? 0.4674 0.3807 0.4712 0.0405  -0.0157 0.0816  48  GLN A C   
373  O O   . GLN A 47  ? 0.4283 0.3520 0.4318 0.0369  -0.0110 0.0884  48  GLN A O   
374  C CB  . GLN A 47  ? 0.3907 0.3191 0.3974 0.0522  -0.0190 0.0586  48  GLN A CB  
375  C CG  . GLN A 47  ? 0.4053 0.3476 0.4079 0.0577  -0.0180 0.0614  48  GLN A CG  
376  C CD  . GLN A 47  ? 0.3962 0.3444 0.3991 0.0694  -0.0228 0.0531  48  GLN A CD  
377  O OE1 . GLN A 47  ? 0.3880 0.3433 0.4004 0.0705  -0.0235 0.0417  48  GLN A OE1 
378  N NE2 . GLN A 47  ? 0.3861 0.3316 0.3792 0.0788  -0.0261 0.0590  48  GLN A NE2 
379  N N   . SER A 48  ? 0.4235 0.3199 0.4238 0.0442  -0.0196 0.0873  49  SER A N   
380  C CA  . SER A 48  ? 0.4873 0.3754 0.4828 0.0441  -0.0178 0.1035  49  SER A CA  
381  C C   . SER A 48  ? 0.5083 0.3731 0.5085 0.0396  -0.0227 0.1084  49  SER A C   
382  O O   . SER A 48  ? 0.4673 0.3199 0.4651 0.0461  -0.0293 0.1014  49  SER A O   
383  C CB  . SER A 48  ? 0.4733 0.3638 0.4561 0.0573  -0.0190 0.1063  49  SER A CB  
384  O OG  . SER A 48  ? 0.5948 0.4715 0.5705 0.0588  -0.0181 0.1223  49  SER A OG  
385  N N   . VAL A 49  ? 0.4857 0.3446 0.4942 0.0288  -0.0202 0.1195  50  VAL A N   
386  C CA  . VAL A 49  ? 0.5174 0.3528 0.5331 0.0234  -0.0264 0.1243  50  VAL A CA  
387  C C   . VAL A 49  ? 0.5615 0.3809 0.5688 0.0307  -0.0288 0.1351  50  VAL A C   
388  O O   . VAL A 49  ? 0.5410 0.3402 0.5480 0.0340  -0.0374 0.1313  50  VAL A O   
389  C CB  . VAL A 49  ? 0.5275 0.3623 0.5581 0.0095  -0.0235 0.1343  50  VAL A CB  
390  C CG1 . VAL A 49  ? 0.5610 0.3700 0.6019 0.0035  -0.0314 0.1397  50  VAL A CG1 
391  C CG2 . VAL A 49  ? 0.5127 0.3607 0.5499 0.0035  -0.0229 0.1224  50  VAL A CG2 
392  N N   . GLN A 50  ? 0.5298 0.3570 0.5285 0.0344  -0.0218 0.1484  51  GLN A N   
393  C CA  . GLN A 50  ? 0.5830 0.3932 0.5714 0.0413  -0.0235 0.1612  51  GLN A CA  
394  C C   . GLN A 50  ? 0.5670 0.3714 0.5431 0.0558  -0.0316 0.1495  51  GLN A C   
395  O O   . GLN A 50  ? 0.6112 0.3945 0.5815 0.0614  -0.0377 0.1551  51  GLN A O   
396  C CB  . GLN A 50  ? 0.6342 0.4556 0.6128 0.0437  -0.0131 0.1780  51  GLN A CB  
397  C CG  . GLN A 50  ? 0.7051 0.5471 0.6686 0.0558  -0.0105 0.1699  51  GLN A CG  
398  C CD  . GLN A 50  ? 0.7555 0.6133 0.7111 0.0568  0.0008  0.1833  51  GLN A CD  
399  O OE1 . GLN A 50  ? 0.7667 0.6353 0.7345 0.0460  0.0082  0.1889  51  GLN A OE1 
400  N NE2 . GLN A 50  ? 0.7563 0.6159 0.6908 0.0711  0.0016  0.1877  51  GLN A NE2 
401  N N   . ASP A 51  ? 0.5542 0.3767 0.5281 0.0620  -0.0320 0.1335  52  ASP A N   
402  C CA  . ASP A 51  ? 0.5711 0.3926 0.5376 0.0757  -0.0392 0.1211  52  ASP A CA  
403  C C   . ASP A 51  ? 0.5092 0.3243 0.4851 0.0753  -0.0459 0.1051  52  ASP A C   
404  O O   . ASP A 51  ? 0.4949 0.3077 0.4676 0.0866  -0.0521 0.0949  52  ASP A O   
405  C CB  . ASP A 51  ? 0.5738 0.4197 0.5352 0.0831  -0.0363 0.1128  52  ASP A CB  
406  C CG  . ASP A 51  ? 0.6473 0.4983 0.5940 0.0891  -0.0316 0.1262  52  ASP A CG  
407  O OD1 . ASP A 51  ? 0.6825 0.5194 0.6161 0.0984  -0.0352 0.1347  52  ASP A OD1 
408  O OD2 . ASP A 51  ? 0.6650 0.5336 0.6118 0.0853  -0.0245 0.1282  52  ASP A OD2 
409  N N   . LYS A 52  ? 0.4637 0.2763 0.4505 0.0638  -0.0449 0.1023  53  LYS A N   
410  C CA  . LYS A 52  ? 0.4454 0.2546 0.4385 0.0641  -0.0497 0.0862  53  LYS A CA  
411  C C   . LYS A 52  ? 0.4499 0.2796 0.4428 0.0722  -0.0479 0.0710  53  LYS A C   
412  O O   . LYS A 52  ? 0.4340 0.2611 0.4285 0.0795  -0.0522 0.0585  53  LYS A O   
413  C CB  . LYS A 52  ? 0.4771 0.2602 0.4692 0.0693  -0.0596 0.0850  53  LYS A CB  
414  C CG  . LYS A 52  ? 0.5016 0.2628 0.4993 0.0589  -0.0629 0.0975  53  LYS A CG  
415  C CD  . LYS A 52  ? 0.5195 0.2786 0.5273 0.0489  -0.0644 0.0901  53  LYS A CD  
416  C CE  . LYS A 52  ? 0.5823 0.3140 0.5984 0.0414  -0.0728 0.0981  53  LYS A CE  
417  N NZ  . LYS A 52  ? 0.5465 0.2741 0.5719 0.0330  -0.0768 0.0894  53  LYS A NZ  
418  N N   . LYS A 53  ? 0.4556 0.3063 0.4480 0.0709  -0.0413 0.0721  54  LYS A N   
419  C CA  . LYS A 53  ? 0.4218 0.2929 0.4179 0.0761  -0.0393 0.0589  54  LYS A CA  
420  C C   . LYS A 53  ? 0.4076 0.2874 0.4108 0.0666  -0.0345 0.0519  54  LYS A C   
421  O O   . LYS A 53  ? 0.4101 0.2936 0.4144 0.0569  -0.0302 0.0585  54  LYS A O   
422  C CB  . LYS A 53  ? 0.4613 0.3485 0.4530 0.0805  -0.0367 0.0628  54  LYS A CB  
423  C CG  . LYS A 53  ? 0.4020 0.3108 0.4009 0.0842  -0.0353 0.0501  54  LYS A CG  
424  C CD  . LYS A 53  ? 0.4588 0.3691 0.4606 0.0970  -0.0416 0.0404  54  LYS A CD  
425  C CE  . LYS A 53  ? 0.5223 0.4555 0.5359 0.0994  -0.0402 0.0288  54  LYS A CE  
426  N NZ  . LYS A 53  ? 0.5734 0.5114 0.5980 0.1079  -0.0437 0.0163  54  LYS A NZ  
427  N N   . ALA A 54  ? 0.3686 0.2516 0.3763 0.0701  -0.0349 0.0389  55  ALA A N   
428  C CA  . ALA A 54  ? 0.3652 0.2542 0.3764 0.0628  -0.0304 0.0323  55  ALA A CA  
429  C C   . ALA A 54  ? 0.3368 0.2485 0.3527 0.0600  -0.0240 0.0296  55  ALA A C   
430  O O   . ALA A 54  ? 0.3363 0.2611 0.3562 0.0667  -0.0239 0.0261  55  ALA A O   
431  C CB  . ALA A 54  ? 0.3633 0.2477 0.3755 0.0689  -0.0318 0.0201  55  ALA A CB  
432  N N   . VAL A 55  ? 0.3244 0.2396 0.3406 0.0504  -0.0199 0.0307  56  VAL A N   
433  C CA  . VAL A 55  ? 0.3058 0.2400 0.3266 0.0473  -0.0144 0.0271  56  VAL A CA  
434  C C   . VAL A 55  ? 0.3037 0.2484 0.3312 0.0532  -0.0118 0.0162  56  VAL A C   
435  O O   . VAL A 55  ? 0.3110 0.2485 0.3372 0.0565  -0.0116 0.0100  56  VAL A O   
436  C CB  . VAL A 55  ? 0.2993 0.2320 0.3182 0.0370  -0.0116 0.0286  56  VAL A CB  
437  C CG1 . VAL A 55  ? 0.2827 0.2324 0.3060 0.0340  -0.0063 0.0242  56  VAL A CG1 
438  C CG2 . VAL A 55  ? 0.3012 0.2281 0.3182 0.0308  -0.0132 0.0395  56  VAL A CG2 
439  N N   . ASN A 56  ? 0.3241 0.2863 0.3599 0.0551  -0.0099 0.0134  57  ASN A N   
440  C CA  . ASN A 56  ? 0.2983 0.2735 0.3454 0.0595  -0.0065 0.0041  57  ASN A CA  
441  C C   . ASN A 56  ? 0.2904 0.2833 0.3476 0.0555  -0.0036 0.0028  57  ASN A C   
442  O O   . ASN A 56  ? 0.2781 0.2723 0.3314 0.0502  -0.0045 0.0081  57  ASN A O   
443  C CB  . ASN A 56  ? 0.3115 0.2871 0.3637 0.0709  -0.0115 -0.0003 57  ASN A CB  
444  C CG  . ASN A 56  ? 0.3479 0.3276 0.4005 0.0757  -0.0178 0.0035  57  ASN A CG  
445  O OD1 . ASN A 56  ? 0.3634 0.3587 0.4262 0.0768  -0.0183 0.0001  57  ASN A OD1 
446  N ND2 . ASN A 56  ? 0.3700 0.3348 0.4107 0.0789  -0.0230 0.0108  57  ASN A ND2 
447  N N   . SER A 57  ? 0.2662 0.2731 0.3381 0.0582  -0.0002 -0.0045 58  SER A N   
448  C CA  . SER A 57  ? 0.2506 0.2732 0.3352 0.0537  0.0020  -0.0061 58  SER A CA  
449  C C   . SER A 57  ? 0.2596 0.2882 0.3475 0.0572  -0.0061 -0.0050 58  SER A C   
450  O O   . SER A 57  ? 0.2493 0.2869 0.3441 0.0529  -0.0065 -0.0053 58  SER A O   
451  C CB  . SER A 57  ? 0.2848 0.3219 0.3884 0.0557  0.0076  -0.0133 58  SER A CB  
452  O OG  . SER A 57  ? 0.3203 0.3614 0.4330 0.0660  0.0031  -0.0187 58  SER A OG  
453  N N   . SER A 58  ? 0.2819 0.3043 0.3636 0.0658  -0.0130 -0.0038 59  SER A N   
454  C CA  . SER A 58  ? 0.2713 0.2972 0.3506 0.0713  -0.0209 -0.0024 59  SER A CA  
455  C C   . SER A 58  ? 0.2627 0.2784 0.3233 0.0686  -0.0214 0.0075  59  SER A C   
456  O O   . SER A 58  ? 0.3020 0.3209 0.3574 0.0735  -0.0266 0.0095  59  SER A O   
457  C CB  . SER A 58  ? 0.3296 0.3544 0.4105 0.0839  -0.0285 -0.0059 59  SER A CB  
458  O OG  . SER A 58  ? 0.3812 0.4194 0.4837 0.0875  -0.0292 -0.0158 59  SER A OG  
459  N N   . THR A 59  ? 0.2699 0.2741 0.3211 0.0614  -0.0164 0.0134  60  THR A N   
460  C CA  . THR A 59  ? 0.2771 0.2733 0.3146 0.0582  -0.0163 0.0234  60  THR A CA  
461  C C   . THR A 59  ? 0.3026 0.3091 0.3407 0.0543  -0.0157 0.0243  60  THR A C   
462  O O   . THR A 59  ? 0.2537 0.2663 0.2992 0.0475  -0.0126 0.0203  60  THR A O   
463  C CB  . THR A 59  ? 0.2698 0.2525 0.3016 0.0504  -0.0124 0.0281  60  THR A CB  
464  O OG1 . THR A 59  ? 0.2908 0.2617 0.3207 0.0553  -0.0145 0.0272  60  THR A OG1 
465  C CG2 . THR A 59  ? 0.2811 0.2583 0.3039 0.0462  -0.0117 0.0388  60  THR A CG2 
466  N N   . ILE A 60  ? 0.2814 0.2890 0.3103 0.0594  -0.0185 0.0298  61  ILE A N   
467  C CA  . ILE A 60  ? 0.2694 0.2861 0.2964 0.0582  -0.0188 0.0306  61  ILE A CA  
468  C C   . ILE A 60  ? 0.2912 0.3025 0.3097 0.0515  -0.0138 0.0406  61  ILE A C   
469  O O   . ILE A 60  ? 0.3031 0.3065 0.3127 0.0538  -0.0125 0.0496  61  ILE A O   
470  C CB  . ILE A 60  ? 0.2601 0.2830 0.2815 0.0706  -0.0255 0.0291  61  ILE A CB  
471  C CG1 . ILE A 60  ? 0.2581 0.2877 0.2925 0.0768  -0.0320 0.0178  61  ILE A CG1 
472  C CG2 . ILE A 60  ? 0.2561 0.2872 0.2726 0.0712  -0.0262 0.0299  61  ILE A CG2 
473  C CD1 . ILE A 60  ? 0.2840 0.3154 0.3110 0.0915  -0.0409 0.0157  61  ILE A CD1 
474  N N   . PHE A 61  ? 0.2442 0.2592 0.2668 0.0429  -0.0111 0.0395  62  PHE A N   
475  C CA  . PHE A 61  ? 0.2549 0.2670 0.2734 0.0360  -0.0071 0.0474  62  PHE A CA  
476  C C   . PHE A 61  ? 0.3137 0.3370 0.3297 0.0381  -0.0075 0.0481  62  PHE A C   
477  O O   . PHE A 61  ? 0.2867 0.3180 0.3067 0.0404  -0.0111 0.0403  62  PHE A O   
478  C CB  . PHE A 61  ? 0.2610 0.2677 0.2849 0.0255  -0.0048 0.0450  62  PHE A CB  
479  C CG  . PHE A 61  ? 0.2840 0.2783 0.3087 0.0233  -0.0042 0.0441  62  PHE A CG  
480  C CD1 . PHE A 61  ? 0.2651 0.2598 0.2942 0.0259  -0.0046 0.0361  62  PHE A CD1 
481  C CD2 . PHE A 61  ? 0.3234 0.3061 0.3458 0.0185  -0.0034 0.0506  62  PHE A CD2 
482  C CE1 . PHE A 61  ? 0.2850 0.2687 0.3135 0.0254  -0.0039 0.0342  62  PHE A CE1 
483  C CE2 . PHE A 61  ? 0.3081 0.2778 0.3302 0.0175  -0.0044 0.0483  62  PHE A CE2 
484  C CZ  . PHE A 61  ? 0.3209 0.2913 0.3448 0.0217  -0.0045 0.0398  62  PHE A CZ  
485  N N   . GLU A 62  ? 0.3185 0.3424 0.3295 0.0367  -0.0038 0.0574  63  GLU A N   
486  C CA  . GLU A 62  ? 0.3314 0.3664 0.3405 0.0383  -0.0033 0.0577  63  GLU A CA  
487  C C   . GLU A 62  ? 0.2803 0.3164 0.2974 0.0291  -0.0038 0.0525  63  GLU A C   
488  O O   . GLU A 62  ? 0.2659 0.2939 0.2874 0.0202  -0.0019 0.0542  63  GLU A O   
489  C CB  . GLU A 62  ? 0.3412 0.3784 0.3449 0.0393  0.0026  0.0700  63  GLU A CB  
490  C CG  . GLU A 62  ? 0.4127 0.4493 0.4043 0.0508  0.0031  0.0758  63  GLU A CG  
491  C CD  . GLU A 62  ? 0.6007 0.6343 0.5887 0.0495  0.0106  0.0910  63  GLU A CD  
492  O OE1 . GLU A 62  ? 0.5991 0.6335 0.5964 0.0398  0.0152  0.0968  63  GLU A OE1 
493  O OE2 . GLU A 62  ? 0.6363 0.6661 0.6127 0.0584  0.0116  0.0976  63  GLU A OE2 
494  N N   . LEU A 63  ? 0.2518 0.2961 0.2700 0.0318  -0.0075 0.0456  64  LEU A N   
495  C CA  . LEU A 63  ? 0.2631 0.3066 0.2875 0.0238  -0.0087 0.0410  64  LEU A CA  
496  C C   . LEU A 63  ? 0.2653 0.3134 0.2896 0.0208  -0.0068 0.0452  64  LEU A C   
497  O O   . LEU A 63  ? 0.2644 0.3092 0.2928 0.0135  -0.0078 0.0428  64  LEU A O   
498  C CB  . LEU A 63  ? 0.2213 0.2694 0.2496 0.0268  -0.0146 0.0315  64  LEU A CB  
499  C CG  . LEU A 63  ? 0.2179 0.2637 0.2520 0.0285  -0.0169 0.0259  64  LEU A CG  
500  C CD1 . LEU A 63  ? 0.2518 0.3019 0.2942 0.0288  -0.0227 0.0175  64  LEU A CD1 
501  C CD2 . LEU A 63  ? 0.2423 0.2786 0.2793 0.0208  -0.0123 0.0273  64  LEU A CD2 
502  N N   . GLY A 64  ? 0.2727 0.2604 0.2767 0.0114  0.0189  0.0010  65  GLY A N   
503  C CA  . GLY A 64  ? 0.3076 0.2971 0.3108 0.0057  0.0192  -0.0014 65  GLY A CA  
504  C C   . GLY A 64  ? 0.2716 0.2732 0.2706 0.0046  0.0134  -0.0007 65  GLY A C   
505  O O   . GLY A 64  ? 0.2300 0.2351 0.2249 0.0079  0.0096  0.0043  65  GLY A O   
506  N N   . SER A 65  ? 0.2629 0.2713 0.2637 -0.0002 0.0128  -0.0061 66  SER A N   
507  C CA  . SER A 65  ? 0.2850 0.3039 0.2828 -0.0012 0.0079  -0.0053 66  SER A CA  
508  C C   . SER A 65  ? 0.2808 0.3076 0.2765 0.0015  0.0040  -0.0041 66  SER A C   
509  O O   . SER A 65  ? 0.2484 0.2811 0.2413 0.0016  0.0004  -0.0013 66  SER A O   
510  C CB  . SER A 65  ? 0.3736 0.3996 0.3748 -0.0058 0.0077  -0.0115 66  SER A CB  
511  O OG  . SER A 65  ? 0.4232 0.4474 0.4253 -0.0080 0.0089  -0.0101 66  SER A OG  
512  N N   . VAL A 66  ? 0.2441 0.2712 0.2419 0.0033  0.0053  -0.0065 67  VAL A N   
513  C CA  . VAL A 66  ? 0.2117 0.2467 0.2085 0.0057  0.0025  -0.0050 67  VAL A CA  
514  C C   . VAL A 66  ? 0.2223 0.2558 0.2171 0.0089  -0.0001 0.0018  67  VAL A C   
515  O O   . VAL A 66  ? 0.2733 0.3139 0.2678 0.0097  -0.0030 0.0039  67  VAL A O   
516  C CB  . VAL A 66  ? 0.2355 0.2710 0.2355 0.0072  0.0055  -0.0097 67  VAL A CB  
517  C CG1 . VAL A 66  ? 0.2079 0.2504 0.2084 0.0105  0.0040  -0.0072 67  VAL A CG1 
518  C CG2 . VAL A 66  ? 0.2691 0.3105 0.2692 0.0036  0.0064  -0.0174 67  VAL A CG2 
519  N N   . SER A 67  ? 0.2183 0.2432 0.2116 0.0103  0.0008  0.0054  68  SER A N   
520  C CA  . SER A 67  ? 0.1855 0.2101 0.1755 0.0129  -0.0025 0.0111  68  SER A CA  
521  C C   . SER A 67  ? 0.2183 0.2494 0.2058 0.0106  -0.0062 0.0119  68  SER A C   
522  O O   . SER A 67  ? 0.2440 0.2784 0.2306 0.0121  -0.0096 0.0148  68  SER A O   
523  C CB  . SER A 67  ? 0.2253 0.2399 0.2118 0.0143  -0.0005 0.0148  68  SER A CB  
524  O OG  . SER A 67  ? 0.2243 0.2310 0.2136 0.0169  0.0034  0.0151  68  SER A OG  
525  N N   . LYS A 68  ? 0.2125 0.2453 0.1996 0.0072  -0.0056 0.0094  69  LYS A N   
526  C CA  . LYS A 68  ? 0.2131 0.2507 0.1987 0.0056  -0.0085 0.0104  69  LYS A CA  
527  C C   . LYS A 68  ? 0.2006 0.2459 0.1881 0.0058  -0.0110 0.0112  69  LYS A C   
528  O O   . LYS A 68  ? 0.2027 0.2500 0.1895 0.0052  -0.0135 0.0132  69  LYS A O   
529  C CB  . LYS A 68  ? 0.2167 0.2562 0.2032 0.0026  -0.0074 0.0076  69  LYS A CB  
530  C CG  . LYS A 68  ? 0.2035 0.2362 0.1894 0.0015  -0.0043 0.0070  69  LYS A CG  
531  C CD  . LYS A 68  ? 0.2667 0.3037 0.2559 -0.0016 -0.0034 0.0033  69  LYS A CD  
532  C CE  . LYS A 68  ? 0.2681 0.2991 0.2582 -0.0033 0.0004  0.0029  69  LYS A CE  
533  N NZ  . LYS A 68  ? 0.2754 0.2990 0.2674 -0.0039 0.0046  0.0014  69  LYS A NZ  
534  N N   . LEU A 69  ? 0.2095 0.2586 0.1996 0.0066  -0.0098 0.0094  70  LEU A N   
535  C CA  . LEU A 69  ? 0.2218 0.2783 0.2140 0.0068  -0.0111 0.0107  70  LEU A CA  
536  C C   . LEU A 69  ? 0.2405 0.2971 0.2346 0.0084  -0.0135 0.0138  70  LEU A C   
537  O O   . LEU A 69  ? 0.2240 0.2856 0.2203 0.0074  -0.0151 0.0155  70  LEU A O   
538  C CB  . LEU A 69  ? 0.2112 0.2720 0.2056 0.0076  -0.0085 0.0077  70  LEU A CB  
539  C CG  . LEU A 69  ? 0.2320 0.2948 0.2244 0.0057  -0.0066 0.0032  70  LEU A CG  
540  C CD1 . LEU A 69  ? 0.1888 0.2562 0.1825 0.0068  -0.0038 -0.0006 70  LEU A CD1 
541  C CD2 . LEU A 69  ? 0.2112 0.2793 0.2011 0.0037  -0.0087 0.0048  70  LEU A CD2 
542  N N   . PHE A 70  ? 0.2164 0.2680 0.2099 0.0110  -0.0137 0.0146  71  PHE A N   
543  C CA  . PHE A 70  ? 0.1914 0.2449 0.1863 0.0128  -0.0170 0.0172  71  PHE A CA  
544  C C   . PHE A 70  ? 0.2227 0.2738 0.2136 0.0112  -0.0199 0.0183  71  PHE A C   
545  O O   . PHE A 70  ? 0.2165 0.2718 0.2095 0.0104  -0.0231 0.0189  71  PHE A O   
546  C CB  . PHE A 70  ? 0.2345 0.2845 0.2300 0.0172  -0.0166 0.0185  71  PHE A CB  
547  C CG  . PHE A 70  ? 0.2483 0.3016 0.2497 0.0194  -0.0140 0.0170  71  PHE A CG  
548  C CD1 . PHE A 70  ? 0.2476 0.3099 0.2555 0.0203  -0.0153 0.0174  71  PHE A CD1 
549  C CD2 . PHE A 70  ? 0.2509 0.2986 0.2521 0.0200  -0.0096 0.0145  71  PHE A CD2 
550  C CE1 . PHE A 70  ? 0.2415 0.3076 0.2550 0.0225  -0.0121 0.0156  71  PHE A CE1 
551  C CE2 . PHE A 70  ? 0.2718 0.3223 0.2783 0.0222  -0.0066 0.0121  71  PHE A CE2 
552  C CZ  . PHE A 70  ? 0.2359 0.2958 0.2484 0.0237  -0.0078 0.0128  71  PHE A CZ  
553  N N   . THR A 71  ? 0.1956 0.2405 0.1813 0.0102  -0.0184 0.0179  72  THR A N   
554  C CA  . THR A 71  ? 0.1750 0.2178 0.1570 0.0086  -0.0201 0.0180  72  THR A CA  
555  C C   . THR A 71  ? 0.1719 0.2192 0.1574 0.0058  -0.0211 0.0174  72  THR A C   
556  O O   . THR A 71  ? 0.1883 0.2359 0.1738 0.0047  -0.0235 0.0173  72  THR A O   
557  C CB  . THR A 71  ? 0.2026 0.2392 0.1803 0.0079  -0.0171 0.0174  72  THR A CB  
558  O OG1 . THR A 71  ? 0.2141 0.2454 0.1892 0.0103  -0.0151 0.0187  72  THR A OG1 
559  C CG2 . THR A 71  ? 0.2260 0.2601 0.1995 0.0068  -0.0180 0.0172  72  THR A CG2 
560  N N   . ALA A 72  ? 0.1809 0.2313 0.1690 0.0048  -0.0191 0.0170  73  ALA A N   
561  C CA  . ALA A 72  ? 0.1956 0.2498 0.1865 0.0028  -0.0194 0.0179  73  ALA A CA  
562  C C   . ALA A 72  ? 0.2023 0.2608 0.1981 0.0022  -0.0210 0.0191  73  ALA A C   
563  O O   . ALA A 72  ? 0.1857 0.2442 0.1839 0.0003  -0.0220 0.0199  73  ALA A O   
564  C CB  . ALA A 72  ? 0.2083 0.2665 0.1997 0.0025  -0.0173 0.0176  73  ALA A CB  
565  N N   . THR A 73  ? 0.1812 0.2436 0.1797 0.0037  -0.0207 0.0189  74  THR A N   
566  C CA  . THR A 73  ? 0.1804 0.2487 0.1854 0.0030  -0.0220 0.0197  74  THR A CA  
567  C C   . THR A 73  ? 0.1915 0.2587 0.1973 0.0024  -0.0259 0.0189  74  THR A C   
568  O O   . THR A 73  ? 0.1884 0.2585 0.1995 -0.0003 -0.0272 0.0189  74  THR A O   
569  C CB  . THR A 73  ? 0.1943 0.2674 0.2028 0.0056  -0.0207 0.0194  74  THR A CB  
570  O OG1 . THR A 73  ? 0.1892 0.2637 0.1962 0.0058  -0.0169 0.0188  74  THR A OG1 
571  C CG2 . THR A 73  ? 0.1781 0.2592 0.1953 0.0048  -0.0216 0.0200  74  THR A CG2 
572  N N   . ALA A 74  ? 0.1896 0.2524 0.1896 0.0047  -0.0277 0.0182  75  ALA A N   
573  C CA  . ALA A 74  ? 0.1937 0.2561 0.1921 0.0043  -0.0317 0.0169  75  ALA A CA  
574  C C   . ALA A 74  ? 0.2054 0.2639 0.2030 0.0009  -0.0318 0.0154  75  ALA A C   
575  O O   . ALA A 74  ? 0.2149 0.2753 0.2156 -0.0013 -0.0346 0.0133  75  ALA A O   
576  C CB  . ALA A 74  ? 0.2135 0.2713 0.2037 0.0078  -0.0327 0.0174  75  ALA A CB  
577  N N   . GLY A 75  ? 0.1972 0.2506 0.1914 0.0005  -0.0287 0.0160  76  GLY A N   
578  C CA  . GLY A 75  ? 0.2032 0.2527 0.1977 -0.0019 -0.0283 0.0150  76  GLY A CA  
579  C C   . GLY A 75  ? 0.2236 0.2759 0.2262 -0.0047 -0.0276 0.0162  76  GLY A C   
580  O O   . GLY A 75  ? 0.1744 0.2241 0.1801 -0.0072 -0.0285 0.0145  76  GLY A O   
581  N N   . GLY A 76  ? 0.1770 0.2341 0.1831 -0.0045 -0.0256 0.0190  77  GLY A N   
582  C CA  . GLY A 76  ? 0.2142 0.2743 0.2278 -0.0072 -0.0241 0.0211  77  GLY A CA  
583  C C   . GLY A 76  ? 0.2101 0.2741 0.2309 -0.0096 -0.0265 0.0190  77  GLY A C   
584  O O   . GLY A 76  ? 0.2129 0.2762 0.2405 -0.0132 -0.0258 0.0191  77  GLY A O   
585  N N   . TYR A 77  ? 0.1861 0.2543 0.2060 -0.0078 -0.0296 0.0169  78  TYR A N   
586  C CA  . TYR A 77  ? 0.1737 0.2481 0.2008 -0.0096 -0.0331 0.0142  78  TYR A CA  
587  C C   . TYR A 77  ? 0.2132 0.2833 0.2393 -0.0121 -0.0362 0.0100  78  TYR A C   
588  O O   . TYR A 77  ? 0.2219 0.2945 0.2566 -0.0163 -0.0373 0.0075  78  TYR A O   
589  C CB  . TYR A 77  ? 0.1814 0.2614 0.2067 -0.0055 -0.0359 0.0138  78  TYR A CB  
590  C CG  . TYR A 77  ? 0.1881 0.2775 0.2217 -0.0065 -0.0404 0.0112  78  TYR A CG  
591  C CD1 . TYR A 77  ? 0.2203 0.3101 0.2507 -0.0067 -0.0459 0.0074  78  TYR A CD1 
592  C CD2 . TYR A 77  ? 0.2182 0.3172 0.2627 -0.0070 -0.0394 0.0123  78  TYR A CD2 
593  C CE1 . TYR A 77  ? 0.2500 0.3502 0.2883 -0.0075 -0.0509 0.0044  78  TYR A CE1 
594  C CE2 . TYR A 77  ? 0.2230 0.3324 0.2768 -0.0077 -0.0438 0.0097  78  TYR A CE2 
595  C CZ  . TYR A 77  ? 0.2683 0.3787 0.3191 -0.0080 -0.0500 0.0057  78  TYR A CZ  
596  O OH  . TYR A 77  ? 0.3022 0.4249 0.3627 -0.0087 -0.0553 0.0026  78  TYR A OH  
597  N N   . ALA A 78  ? 0.2042 0.2681 0.2200 -0.0098 -0.0373 0.0085  79  ALA A N   
598  C CA  . ALA A 78  ? 0.2070 0.2664 0.2200 -0.0118 -0.0397 0.0037  79  ALA A CA  
599  C C   . ALA A 78  ? 0.2187 0.2721 0.2375 -0.0157 -0.0367 0.0031  79  ALA A C   
600  O O   . ALA A 78  ? 0.2308 0.2833 0.2546 -0.0194 -0.0384 -0.0016 79  ALA A O   
601  C CB  . ALA A 78  ? 0.2370 0.2906 0.2375 -0.0083 -0.0396 0.0032  79  ALA A CB  
602  N N   . LYS A 79  ? 0.2147 0.2638 0.2331 -0.0147 -0.0322 0.0078  80  LYS A N   
603  C CA  . LYS A 79  ? 0.2322 0.2747 0.2557 -0.0172 -0.0291 0.0087  80  LYS A CA  
604  C C   . LYS A 79  ? 0.2688 0.3145 0.3043 -0.0217 -0.0281 0.0094  80  LYS A C   
605  O O   . LYS A 79  ? 0.2332 0.2735 0.2751 -0.0254 -0.0273 0.0069  80  LYS A O   
606  C CB  . LYS A 79  ? 0.2289 0.2683 0.2490 -0.0143 -0.0253 0.0143  80  LYS A CB  
607  C CG  . LYS A 79  ? 0.2383 0.2710 0.2634 -0.0154 -0.0218 0.0173  80  LYS A CG  
608  C CD  . LYS A 79  ? 0.2691 0.3054 0.3006 -0.0168 -0.0188 0.0233  80  LYS A CD  
609  C CE  . LYS A 79  ? 0.2922 0.3212 0.3284 -0.0173 -0.0149 0.0281  80  LYS A CE  
610  N NZ  . LYS A 79  ? 0.2969 0.3299 0.3387 -0.0191 -0.0116 0.0343  80  LYS A NZ  
611  N N   . ASN A 80  ? 0.2015 0.2558 0.2411 -0.0217 -0.0277 0.0125  81  ASN A N   
612  C CA  . ASN A 80  ? 0.2386 0.2966 0.2905 -0.0262 -0.0257 0.0138  81  ASN A CA  
613  C C   . ASN A 80  ? 0.2478 0.3112 0.3078 -0.0302 -0.0299 0.0072  81  ASN A C   
614  O O   . ASN A 80  ? 0.2440 0.3097 0.3163 -0.0353 -0.0281 0.0069  81  ASN A O   
615  C CB  . ASN A 80  ? 0.2245 0.2903 0.2780 -0.0246 -0.0227 0.0193  81  ASN A CB  
616  C CG  . ASN A 80  ? 0.2997 0.3609 0.3488 -0.0227 -0.0178 0.0259  81  ASN A CG  
617  O OD1 . ASN A 80  ? 0.2979 0.3598 0.3381 -0.0184 -0.0176 0.0278  81  ASN A OD1 
618  N ND2 . ASN A 80  ? 0.2341 0.2903 0.2895 -0.0257 -0.0139 0.0295  81  ASN A ND2 
619  N N   . LYS A 81  ? 0.2375 0.3033 0.2910 -0.0282 -0.0353 0.0021  82  LYS A N   
620  C CA  . LYS A 81  ? 0.2380 0.3090 0.2970 -0.0317 -0.0406 -0.0053 82  LYS A CA  
621  C C   . LYS A 81  ? 0.2591 0.3207 0.3151 -0.0341 -0.0416 -0.0116 82  LYS A C   
622  O O   . LYS A 81  ? 0.2969 0.3627 0.3561 -0.0372 -0.0463 -0.0191 82  LYS A O   
623  C CB  . LYS A 81  ? 0.2682 0.3483 0.3209 -0.0274 -0.0463 -0.0070 82  LYS A CB  
624  C CG  . LYS A 81  ? 0.3347 0.4281 0.3978 -0.0275 -0.0476 -0.0055 82  LYS A CG  
625  C CD  . LYS A 81  ? 0.4268 0.5299 0.4872 -0.0246 -0.0550 -0.0093 82  LYS A CD  
626  C CE  . LYS A 81  ? 0.4346 0.5525 0.5102 -0.0267 -0.0577 -0.0108 82  LYS A CE  
627  N NZ  . LYS A 81  ? 0.4702 0.5983 0.5419 -0.0221 -0.0653 -0.0130 82  LYS A NZ  
628  N N   . GLY A 82  ? 0.2906 0.3407 0.3410 -0.0326 -0.0374 -0.0090 83  GLY A N   
629  C CA  . GLY A 82  ? 0.2781 0.3186 0.3261 -0.0343 -0.0373 -0.0150 83  GLY A CA  
630  C C   . GLY A 82  ? 0.2882 0.3285 0.3228 -0.0309 -0.0413 -0.0201 83  GLY A C   
631  O O   . GLY A 82  ? 0.2671 0.3010 0.2994 -0.0325 -0.0416 -0.0269 83  GLY A O   
632  N N   . LYS A 83  ? 0.2126 0.2594 0.2382 -0.0262 -0.0437 -0.0171 84  LYS A N   
633  C CA  . LYS A 83  ? 0.2563 0.3027 0.2681 -0.0225 -0.0466 -0.0203 84  LYS A CA  
634  C C   . LYS A 83  ? 0.2529 0.2893 0.2562 -0.0195 -0.0420 -0.0185 84  LYS A C   
635  O O   . LYS A 83  ? 0.2453 0.2787 0.2385 -0.0179 -0.0429 -0.0227 84  LYS A O   
636  C CB  . LYS A 83  ? 0.2411 0.2964 0.2472 -0.0183 -0.0498 -0.0165 84  LYS A CB  
637  C CG  . LYS A 83  ? 0.2620 0.3295 0.2769 -0.0201 -0.0549 -0.0183 84  LYS A CG  
638  C CD  . LYS A 83  ? 0.2995 0.3714 0.3132 -0.0227 -0.0609 -0.0271 84  LYS A CD  
639  C CE  . LYS A 83  ? 0.3826 0.4686 0.4076 -0.0249 -0.0663 -0.0292 84  LYS A CE  
640  N NZ  . LYS A 83  ? 0.4392 0.5324 0.4614 -0.0265 -0.0736 -0.0380 84  LYS A NZ  
641  N N   . ILE A 84  ? 0.2325 0.2648 0.2394 -0.0184 -0.0373 -0.0121 85  ILE A N   
642  C CA  . ILE A 84  ? 0.2527 0.2767 0.2550 -0.0158 -0.0329 -0.0103 85  ILE A CA  
643  C C   . ILE A 84  ? 0.2867 0.3058 0.2987 -0.0173 -0.0289 -0.0063 85  ILE A C   
644  O O   . ILE A 84  ? 0.2329 0.2554 0.2534 -0.0197 -0.0286 -0.0032 85  ILE A O   
645  C CB  . ILE A 84  ? 0.2336 0.2594 0.2278 -0.0113 -0.0316 -0.0052 85  ILE A CB  
646  C CG1 . ILE A 84  ? 0.2361 0.2674 0.2353 -0.0109 -0.0310 0.0010  85  ILE A CG1 
647  C CG2 . ILE A 84  ? 0.2230 0.2522 0.2069 -0.0091 -0.0345 -0.0074 85  ILE A CG2 
648  C CD1 . ILE A 84  ? 0.2482 0.2810 0.2410 -0.0072 -0.0295 0.0048  85  ILE A CD1 
649  N N   . SER A 85  ? 0.2572 0.2686 0.2679 -0.0153 -0.0254 -0.0058 86  SER A N   
650  C CA  . SER A 85  ? 0.2412 0.2487 0.2583 -0.0143 -0.0214 0.0004  86  SER A CA  
651  C C   . SER A 85  ? 0.2702 0.2788 0.2810 -0.0096 -0.0198 0.0042  86  SER A C   
652  O O   . SER A 85  ? 0.2424 0.2501 0.2462 -0.0076 -0.0199 0.0007  86  SER A O   
653  C CB  . SER A 85  ? 0.2777 0.2750 0.3016 -0.0158 -0.0187 -0.0025 86  SER A CB  
654  O OG  . SER A 85  ? 0.3582 0.3511 0.3858 -0.0127 -0.0148 0.0041  86  SER A OG  
655  N N   . PHE A 86  ? 0.2573 0.2688 0.2707 -0.0079 -0.0182 0.0112  87  PHE A N   
656  C CA  . PHE A 86  ? 0.2533 0.2675 0.2621 -0.0040 -0.0172 0.0140  87  PHE A CA  
657  C C   . PHE A 86  ? 0.2669 0.2750 0.2768 -0.0014 -0.0147 0.0127  87  PHE A C   
658  O O   . PHE A 86  ? 0.2727 0.2834 0.2792 0.0014  -0.0140 0.0130  87  PHE A O   
659  C CB  . PHE A 86  ? 0.2747 0.2944 0.2854 -0.0027 -0.0166 0.0210  87  PHE A CB  
660  C CG  . PHE A 86  ? 0.2492 0.2762 0.2581 -0.0042 -0.0182 0.0219  87  PHE A CG  
661  C CD1 . PHE A 86  ? 0.3003 0.3297 0.3041 -0.0047 -0.0203 0.0179  87  PHE A CD1 
662  C CD2 . PHE A 86  ? 0.2764 0.3075 0.2885 -0.0048 -0.0173 0.0270  87  PHE A CD2 
663  C CE1 . PHE A 86  ? 0.3069 0.3426 0.3102 -0.0053 -0.0216 0.0188  87  PHE A CE1 
664  C CE2 . PHE A 86  ? 0.2636 0.3015 0.2747 -0.0058 -0.0182 0.0274  87  PHE A CE2 
665  C CZ  . PHE A 86  ? 0.2995 0.3396 0.3069 -0.0059 -0.0204 0.0231  87  PHE A CZ  
666  N N   . ASP A 87  ? 0.2248 0.2250 0.2405 -0.0023 -0.0131 0.0111  88  ASP A N   
667  C CA  . ASP A 87  ? 0.2595 0.2532 0.2770 0.0005  -0.0104 0.0088  88  ASP A CA  
668  C C   . ASP A 87  ? 0.2629 0.2539 0.2742 -0.0001 -0.0104 0.0003  88  ASP A C   
669  O O   . ASP A 87  ? 0.2867 0.2733 0.2988 0.0026  -0.0075 -0.0023 88  ASP A O   
670  C CB  . ASP A 87  ? 0.2832 0.2677 0.3101 0.0001  -0.0079 0.0102  88  ASP A CB  
671  C CG  . ASP A 87  ? 0.4215 0.4075 0.4535 0.0028  -0.0066 0.0199  88  ASP A CG  
672  O OD1 . ASP A 87  ? 0.3800 0.3747 0.4082 0.0054  -0.0078 0.0244  88  ASP A OD1 
673  O OD2 . ASP A 87  ? 0.5125 0.4908 0.5522 0.0024  -0.0041 0.0231  88  ASP A OD2 
674  N N   . ASP A 88  ? 0.2691 0.2634 0.2742 -0.0030 -0.0134 -0.0037 89  ASP A N   
675  C CA  . ASP A 88  ? 0.3020 0.2950 0.2989 -0.0031 -0.0136 -0.0109 89  ASP A CA  
676  C C   . ASP A 88  ? 0.2704 0.2669 0.2608 0.0004  -0.0116 -0.0096 89  ASP A C   
677  O O   . ASP A 88  ? 0.2607 0.2622 0.2522 0.0019  -0.0114 -0.0039 89  ASP A O   
678  C CB  . ASP A 88  ? 0.2636 0.2610 0.2548 -0.0062 -0.0180 -0.0142 89  ASP A CB  
679  C CG  . ASP A 88  ? 0.3179 0.3128 0.3163 -0.0105 -0.0200 -0.0179 89  ASP A CG  
680  O OD1 . ASP A 88  ? 0.3163 0.3033 0.3221 -0.0116 -0.0174 -0.0202 89  ASP A OD1 
681  O OD2 . ASP A 88  ? 0.3512 0.3522 0.3485 -0.0130 -0.0241 -0.0188 89  ASP A OD2 
682  N N   . THR A 89  ? 0.3018 0.2958 0.2851 0.0012  -0.0098 -0.0153 90  THR A N   
683  C CA  . THR A 89  ? 0.2414 0.2386 0.2184 0.0036  -0.0072 -0.0143 90  THR A CA  
684  C C   . THR A 89  ? 0.2756 0.2755 0.2405 0.0027  -0.0091 -0.0163 90  THR A C   
685  O O   . THR A 89  ? 0.2929 0.2924 0.2539 0.0006  -0.0126 -0.0202 90  THR A O   
686  C CB  . THR A 89  ? 0.3159 0.3089 0.2949 0.0063  -0.0021 -0.0179 90  THR A CB  
687  O OG1 . THR A 89  ? 0.3143 0.3018 0.2887 0.0052  -0.0016 -0.0259 90  THR A OG1 
688  C CG2 . THR A 89  ? 0.3226 0.3135 0.3143 0.0083  -0.0006 -0.0144 90  THR A CG2 
689  N N   . PRO A 90  ? 0.2780 0.2812 0.2373 0.0042  -0.0071 -0.0134 91  PRO A N   
690  C CA  . PRO A 90  ? 0.3053 0.3108 0.2534 0.0039  -0.0092 -0.0130 91  PRO A CA  
691  C C   . PRO A 90  ? 0.3078 0.3111 0.2447 0.0041  -0.0092 -0.0191 91  PRO A C   
692  O O   . PRO A 90  ? 0.3480 0.3539 0.2766 0.0038  -0.0131 -0.0194 91  PRO A O   
693  C CB  . PRO A 90  ? 0.2951 0.3027 0.2414 0.0053  -0.0055 -0.0083 91  PRO A CB  
694  C CG  . PRO A 90  ? 0.2725 0.2794 0.2262 0.0064  -0.0008 -0.0090 91  PRO A CG  
695  C CD  . PRO A 90  ? 0.2726 0.2780 0.2362 0.0060  -0.0030 -0.0099 91  PRO A CD  
696  N N   . GLY A 91  ? 0.3221 0.3215 0.2586 0.0049  -0.0051 -0.0242 92  GLY A N   
697  C CA  . GLY A 91  ? 0.3310 0.3287 0.2558 0.0050  -0.0047 -0.0311 92  GLY A CA  
698  C C   . GLY A 91  ? 0.3587 0.3559 0.2835 0.0024  -0.0103 -0.0374 92  GLY A C   
699  O O   . GLY A 91  ? 0.3417 0.3394 0.2553 0.0022  -0.0116 -0.0437 92  GLY A O   
700  N N   . LYS A 92  ? 0.3065 0.3033 0.2436 0.0002  -0.0134 -0.0361 93  LYS A N   
701  C CA  . LYS A 92  ? 0.3501 0.3475 0.2893 -0.0032 -0.0189 -0.0416 93  LYS A CA  
702  C C   . LYS A 92  ? 0.3511 0.3562 0.2813 -0.0035 -0.0248 -0.0404 93  LYS A C   
703  O O   . LYS A 92  ? 0.3431 0.3510 0.2700 -0.0057 -0.0295 -0.0471 93  LYS A O   
704  C CB  . LYS A 92  ? 0.3351 0.3308 0.2901 -0.0055 -0.0198 -0.0385 93  LYS A CB  
705  C CG  . LYS A 92  ? 0.3127 0.3094 0.2734 -0.0100 -0.0247 -0.0436 93  LYS A CG  
706  C CD  . LYS A 92  ? 0.3725 0.3656 0.3487 -0.0119 -0.0235 -0.0395 93  LYS A CD  
707  C CE  . LYS A 92  ? 0.3987 0.3924 0.3831 -0.0172 -0.0273 -0.0444 93  LYS A CE  
708  N NZ  . LYS A 92  ? 0.5587 0.5448 0.5448 -0.0196 -0.0258 -0.0546 93  LYS A NZ  
709  N N   . TYR A 93  ? 0.3163 0.3252 0.2431 -0.0011 -0.0246 -0.0323 94  TYR A N   
710  C CA  . TYR A 93  ? 0.3653 0.3811 0.2856 -0.0003 -0.0299 -0.0292 94  TYR A CA  
711  C C   . TYR A 93  ? 0.3739 0.3906 0.2788 0.0034  -0.0279 -0.0262 94  TYR A C   
712  O O   . TYR A 93  ? 0.3324 0.3540 0.2271 0.0046  -0.0325 -0.0271 94  TYR A O   
713  C CB  . TYR A 93  ? 0.3091 0.3277 0.2393 -0.0004 -0.0311 -0.0218 94  TYR A CB  
714  C CG  . TYR A 93  ? 0.2885 0.3065 0.2331 -0.0040 -0.0324 -0.0236 94  TYR A CG  
715  C CD1 . TYR A 93  ? 0.3009 0.3237 0.2503 -0.0069 -0.0379 -0.0271 94  TYR A CD1 
716  C CD2 . TYR A 93  ? 0.2719 0.2847 0.2254 -0.0043 -0.0278 -0.0216 94  TYR A CD2 
717  C CE1 . TYR A 93  ? 0.2848 0.3063 0.2478 -0.0106 -0.0380 -0.0283 94  TYR A CE1 
718  C CE2 . TYR A 93  ? 0.2849 0.2962 0.2508 -0.0073 -0.0283 -0.0220 94  TYR A CE2 
719  C CZ  . TYR A 93  ? 0.2819 0.2970 0.2525 -0.0106 -0.0330 -0.0252 94  TYR A CZ  
720  O OH  . TYR A 93  ? 0.3609 0.3739 0.3443 -0.0140 -0.0326 -0.0252 94  TYR A OH  
721  N N   . TRP A 94  ? 0.3223 0.3348 0.2259 0.0052  -0.0212 -0.0223 95  TRP A N   
722  C CA  . TRP A 94  ? 0.3409 0.3527 0.2306 0.0082  -0.0174 -0.0192 95  TRP A CA  
723  C C   . TRP A 94  ? 0.3542 0.3625 0.2376 0.0084  -0.0126 -0.0259 95  TRP A C   
724  O O   . TRP A 94  ? 0.3314 0.3359 0.2205 0.0085  -0.0063 -0.0259 95  TRP A O   
725  C CB  . TRP A 94  ? 0.3393 0.3494 0.2333 0.0094  -0.0126 -0.0111 95  TRP A CB  
726  C CG  . TRP A 94  ? 0.3362 0.3457 0.2174 0.0123  -0.0096 -0.0056 95  TRP A CG  
727  C CD1 . TRP A 94  ? 0.4004 0.4110 0.2653 0.0145  -0.0104 -0.0063 95  TRP A CD1 
728  C CD2 . TRP A 94  ? 0.3066 0.3138 0.1900 0.0132  -0.0051 0.0019  95  TRP A CD2 
729  N NE1 . TRP A 94  ? 0.3706 0.3791 0.2273 0.0171  -0.0062 0.0014  95  TRP A NE1 
730  C CE2 . TRP A 94  ? 0.3517 0.3576 0.2203 0.0160  -0.0027 0.0061  95  TRP A CE2 
731  C CE3 . TRP A 94  ? 0.3251 0.3315 0.2215 0.0117  -0.0028 0.0050  95  TRP A CE3 
732  C CZ2 . TRP A 94  ? 0.3391 0.3414 0.2069 0.0172  0.0026  0.0137  95  TRP A CZ2 
733  C CZ3 . TRP A 94  ? 0.3427 0.3465 0.2384 0.0125  0.0019  0.0111  95  TRP A CZ3 
734  C CH2 . TRP A 94  ? 0.3641 0.3651 0.2461 0.0151  0.0049  0.0156  95  TRP A CH2 
735  N N   . LYS A 95  ? 0.3425 0.3528 0.2141 0.0085  -0.0158 -0.0323 96  LYS A N   
736  C CA  . LYS A 95  ? 0.3644 0.3714 0.2320 0.0080  -0.0123 -0.0414 96  LYS A CA  
737  C C   . LYS A 95  ? 0.3790 0.3828 0.2395 0.0104  -0.0032 -0.0396 96  LYS A C   
738  O O   . LYS A 95  ? 0.3324 0.3324 0.1957 0.0103  0.0019  -0.0458 96  LYS A O   
739  C CB  . LYS A 95  ? 0.4273 0.4386 0.2818 0.0076  -0.0180 -0.0492 96  LYS A CB  
740  C CG  . LYS A 95  ? 0.5030 0.5194 0.3653 0.0048  -0.0272 -0.0514 96  LYS A CG  
741  C CD  . LYS A 95  ? 0.4725 0.4844 0.3525 0.0008  -0.0273 -0.0568 96  LYS A CD  
742  C CE  . LYS A 95  ? 0.4921 0.5098 0.3795 -0.0028 -0.0360 -0.0606 96  LYS A CE  
743  N NZ  . LYS A 95  ? 0.5777 0.6014 0.4526 -0.0036 -0.0416 -0.0699 96  LYS A NZ  
744  N N   . GLU A 96  ? 0.3447 0.3497 0.1972 0.0127  -0.0004 -0.0311 97  GLU A N   
745  C CA  . GLU A 96  ? 0.3404 0.3429 0.1878 0.0144  0.0091  -0.0290 97  GLU A CA  
746  C C   . GLU A 96  ? 0.3276 0.3274 0.1922 0.0134  0.0146  -0.0275 97  GLU A C   
747  O O   . GLU A 96  ? 0.3608 0.3594 0.2245 0.0144  0.0228  -0.0276 97  GLU A O   
748  C CB  . GLU A 96  ? 0.3912 0.3945 0.2267 0.0167  0.0113  -0.0196 97  GLU A CB  
749  C CG  . GLU A 96  ? 0.4297 0.4362 0.2447 0.0191  0.0073  -0.0202 97  GLU A CG  
750  C CD  . GLU A 96  ? 0.5650 0.5757 0.3795 0.0199  -0.0021 -0.0158 97  GLU A CD  
751  O OE1 . GLU A 96  ? 0.6436 0.6561 0.4439 0.0233  -0.0030 -0.0092 97  GLU A OE1 
752  O OE2 . GLU A 96  ? 0.4883 0.5005 0.3169 0.0175  -0.0081 -0.0183 97  GLU A OE2 
753  N N   . LEU A 97  ? 0.2981 0.2981 0.1782 0.0117  0.0104  -0.0261 98  LEU A N   
754  C CA  . LEU A 97  ? 0.3012 0.3001 0.1972 0.0112  0.0144  -0.0252 98  LEU A CA  
755  C C   . LEU A 97  ? 0.3139 0.3100 0.2180 0.0111  0.0150  -0.0328 98  LEU A C   
756  O O   . LEU A 97  ? 0.3338 0.3294 0.2516 0.0115  0.0177  -0.0319 98  LEU A O   
757  C CB  . LEU A 97  ? 0.2653 0.2662 0.1730 0.0099  0.0102  -0.0191 98  LEU A CB  
758  C CG  . LEU A 97  ? 0.2789 0.2813 0.1820 0.0102  0.0108  -0.0115 98  LEU A CG  
759  C CD1 . LEU A 97  ? 0.2648 0.2692 0.1796 0.0089  0.0068  -0.0070 98  LEU A CD1 
760  C CD2 . LEU A 97  ? 0.3287 0.3305 0.2302 0.0109  0.0193  -0.0091 98  LEU A CD2 
761  N N   . LYS A 98  ? 0.3418 0.3360 0.2383 0.0106  0.0125  -0.0404 99  LYS A N   
762  C CA  . LYS A 98  ? 0.3520 0.3417 0.2571 0.0104  0.0139  -0.0481 99  LYS A CA  
763  C C   . LYS A 98  ? 0.3705 0.3586 0.2773 0.0130  0.0229  -0.0504 99  LYS A C   
764  O O   . LYS A 98  ? 0.3461 0.3361 0.2413 0.0144  0.0279  -0.0501 99  LYS A O   
765  C CB  . LYS A 98  ? 0.4085 0.3966 0.3045 0.0088  0.0099  -0.0575 99  LYS A CB  
766  C CG  . LYS A 98  ? 0.4892 0.4773 0.3925 0.0056  0.0020  -0.0584 99  LYS A CG  
767  C CD  . LYS A 98  ? 0.5274 0.5121 0.4286 0.0034  -0.0001 -0.0703 99  LYS A CD  
768  C CE  . LYS A 98  ? 0.5518 0.5364 0.4635 -0.0005 -0.0072 -0.0713 99  LYS A CE  
769  N NZ  . LYS A 98  ? 0.5185 0.5113 0.4244 -0.0014 -0.0141 -0.0659 99  LYS A NZ  
770  N N   . ASN A 99  ? 0.4038 0.3886 0.3256 0.0140  0.0253  -0.0524 100 ASN A N   
771  C CA  . ASN A 99  ? 0.4196 0.4036 0.3456 0.0171  0.0338  -0.0555 100 ASN A CA  
772  C C   . ASN A 99  ? 0.3748 0.3648 0.3025 0.0183  0.0388  -0.0484 100 ASN A C   
773  O O   . ASN A 99  ? 0.3847 0.3760 0.3100 0.0203  0.0466  -0.0507 100 ASN A O   
774  C CB  . ASN A 99  ? 0.4838 0.4649 0.3963 0.0179  0.0379  -0.0653 100 ASN A CB  
775  C CG  . ASN A 99  ? 0.5489 0.5237 0.4621 0.0164  0.0341  -0.0745 100 ASN A CG  
776  O OD1 . ASN A 99  ? 0.5493 0.5200 0.4772 0.0158  0.0313  -0.0740 100 ASN A OD1 
777  N ND2 . ASN A 99  ? 0.5669 0.5410 0.4641 0.0156  0.0340  -0.0831 100 ASN A ND2 
778  N N   . THR A 100 ? 0.3816 0.3754 0.3134 0.0168  0.0348  -0.0402 101 THR A N   
779  C CA  . THR A 100 ? 0.3463 0.3456 0.2838 0.0171  0.0391  -0.0341 101 THR A CA  
780  C C   . THR A 100 ? 0.2951 0.2974 0.2502 0.0173  0.0359  -0.0298 101 THR A C   
781  O O   . THR A 100 ? 0.2893 0.2891 0.2489 0.0168  0.0299  -0.0294 101 THR A O   
782  C CB  . THR A 100 ? 0.3348 0.3359 0.2609 0.0151  0.0380  -0.0283 101 THR A CB  
783  O OG1 . THR A 100 ? 0.3130 0.3143 0.2415 0.0133  0.0300  -0.0243 101 THR A OG1 
784  C CG2 . THR A 100 ? 0.3234 0.3220 0.2302 0.0154  0.0396  -0.0317 101 THR A CG2 
785  N N   . PRO A 101 ? 0.2807 0.2892 0.2460 0.0181  0.0400  -0.0265 102 PRO A N   
786  C CA  . PRO A 101 ? 0.2795 0.2924 0.2607 0.0189  0.0365  -0.0228 102 PRO A CA  
787  C C   . PRO A 101 ? 0.2810 0.2944 0.2618 0.0165  0.0291  -0.0180 102 PRO A C   
788  O O   . PRO A 101 ? 0.2565 0.2710 0.2470 0.0175  0.0250  -0.0160 102 PRO A O   
789  C CB  . PRO A 101 ? 0.2524 0.2737 0.2425 0.0191  0.0420  -0.0209 102 PRO A CB  
790  C CG  . PRO A 101 ? 0.2881 0.3078 0.2705 0.0199  0.0501  -0.0251 102 PRO A CG  
791  C CD  . PRO A 101 ? 0.3034 0.3158 0.2672 0.0183  0.0482  -0.0266 102 PRO A CD  
792  N N   . ILE A 102 ? 0.2524 0.2652 0.2227 0.0138  0.0275  -0.0156 103 ILE A N   
793  C CA  . ILE A 102 ? 0.2496 0.2633 0.2206 0.0119  0.0209  -0.0115 103 ILE A CA  
794  C C   . ILE A 102 ? 0.2821 0.2910 0.2516 0.0119  0.0155  -0.0131 103 ILE A C   
795  O O   . ILE A 102 ? 0.2370 0.2472 0.2110 0.0109  0.0106  -0.0099 103 ILE A O   
796  C CB  . ILE A 102 ? 0.2310 0.2445 0.1922 0.0097  0.0209  -0.0084 103 ILE A CB  
797  C CG1 . ILE A 102 ? 0.2535 0.2690 0.2178 0.0081  0.0152  -0.0044 103 ILE A CG1 
798  C CG2 . ILE A 102 ? 0.2959 0.3042 0.2419 0.0098  0.0205  -0.0105 103 ILE A CG2 
799  C CD1 . ILE A 102 ? 0.2533 0.2752 0.2293 0.0075  0.0155  -0.0021 103 ILE A CD1 
800  N N   . ASP A 103 ? 0.2596 0.2632 0.2237 0.0126  0.0169  -0.0186 104 ASP A N   
801  C CA  . ASP A 103 ? 0.2869 0.2857 0.2516 0.0119  0.0124  -0.0213 104 ASP A CA  
802  C C   . ASP A 103 ? 0.3006 0.2981 0.2791 0.0136  0.0122  -0.0203 104 ASP A C   
803  O O   . ASP A 103 ? 0.3205 0.3126 0.3016 0.0129  0.0098  -0.0225 104 ASP A O   
804  C CB  . ASP A 103 ? 0.2862 0.2799 0.2409 0.0118  0.0140  -0.0288 104 ASP A CB  
805  C CG  . ASP A 103 ? 0.3396 0.3299 0.2917 0.0093  0.0082  -0.0320 104 ASP A CG  
806  O OD1 . ASP A 103 ? 0.3297 0.3224 0.2845 0.0075  0.0032  -0.0275 104 ASP A OD1 
807  O OD2 . ASP A 103 ? 0.3771 0.3627 0.3255 0.0089  0.0087  -0.0396 104 ASP A OD2 
808  N N   . GLN A 104 ? 0.2588 0.2612 0.2468 0.0160  0.0147  -0.0169 105 GLN A N   
809  C CA  . GLN A 104 ? 0.2446 0.2474 0.2455 0.0185  0.0137  -0.0139 105 GLN A CA  
810  C C   . GLN A 104 ? 0.2415 0.2498 0.2463 0.0175  0.0089  -0.0071 105 GLN A C   
811  O O   . GLN A 104 ? 0.2367 0.2456 0.2504 0.0198  0.0074  -0.0034 105 GLN A O   
812  C CB  . GLN A 104 ? 0.2637 0.2706 0.2735 0.0226  0.0187  -0.0144 105 GLN A CB  
813  C CG  . GLN A 104 ? 0.2936 0.2945 0.3008 0.0243  0.0244  -0.0216 105 GLN A CG  
814  C CD  . GLN A 104 ? 0.2985 0.3053 0.3130 0.0278  0.0305  -0.0228 105 GLN A CD  
815  O OE1 . GLN A 104 ? 0.3248 0.3401 0.3404 0.0269  0.0318  -0.0203 105 GLN A OE1 
816  N NE2 . GLN A 104 ? 0.3259 0.3281 0.3461 0.0316  0.0349  -0.0273 105 GLN A NE2 
817  N N   . VAL A 105 ? 0.2097 0.2219 0.2077 0.0146  0.0068  -0.0054 106 VAL A N   
818  C CA  . VAL A 105 ? 0.1958 0.2131 0.1959 0.0134  0.0026  -0.0002 106 VAL A CA  
819  C C   . VAL A 105 ? 0.2097 0.2227 0.2051 0.0109  -0.0012 0.0001  106 VAL A C   
820  O O   . VAL A 105 ? 0.2341 0.2435 0.2212 0.0090  -0.0015 -0.0033 106 VAL A O   
821  C CB  . VAL A 105 ? 0.1988 0.2222 0.1958 0.0117  0.0033  0.0008  106 VAL A CB  
822  C CG1 . VAL A 105 ? 0.1825 0.2119 0.1825 0.0107  -0.0005 0.0050  106 VAL A CG1 
823  C CG2 . VAL A 105 ? 0.1916 0.2195 0.1938 0.0133  0.0080  -0.0007 106 VAL A CG2 
824  N N   . ASN A 106 ? 0.1986 0.2128 0.1991 0.0108  -0.0041 0.0043  107 ASN A N   
825  C CA  . ASN A 106 ? 0.2094 0.2206 0.2072 0.0080  -0.0072 0.0044  107 ASN A CA  
826  C C   . ASN A 106 ? 0.2284 0.2451 0.2219 0.0061  -0.0098 0.0068  107 ASN A C   
827  O O   . ASN A 106 ? 0.2235 0.2456 0.2164 0.0066  -0.0093 0.0084  107 ASN A O   
828  C CB  . ASN A 106 ? 0.2053 0.2129 0.2109 0.0085  -0.0078 0.0075  107 ASN A CB  
829  C CG  . ASN A 106 ? 0.2319 0.2458 0.2421 0.0102  -0.0090 0.0144  107 ASN A CG  
830  O OD1 . ASN A 106 ? 0.2439 0.2648 0.2512 0.0093  -0.0107 0.0163  107 ASN A OD1 
831  N ND2 . ASN A 106 ? 0.2411 0.2522 0.2584 0.0127  -0.0080 0.0181  107 ASN A ND2 
832  N N   . LEU A 107 ? 0.2074 0.2228 0.1989 0.0037  -0.0125 0.0065  108 LEU A N   
833  C CA  . LEU A 107 ? 0.2148 0.2347 0.2022 0.0024  -0.0146 0.0079  108 LEU A CA  
834  C C   . LEU A 107 ? 0.1795 0.2052 0.1706 0.0028  -0.0152 0.0125  108 LEU A C   
835  O O   . LEU A 107 ? 0.1740 0.2037 0.1624 0.0027  -0.0153 0.0131  108 LEU A O   
836  C CB  . LEU A 107 ? 0.2038 0.2225 0.1900 0.0001  -0.0176 0.0063  108 LEU A CB  
837  C CG  . LEU A 107 ? 0.2483 0.2626 0.2296 -0.0007 -0.0181 0.0006  108 LEU A CG  
838  C CD1 . LEU A 107 ? 0.2141 0.2306 0.1950 -0.0032 -0.0221 -0.0010 108 LEU A CD1 
839  C CD2 . LEU A 107 ? 0.2328 0.2465 0.2051 0.0010  -0.0162 -0.0013 108 LEU A CD2 
840  N N   . LEU A 108 ? 0.2008 0.2272 0.1978 0.0034  -0.0153 0.0158  109 LEU A N   
841  C CA  . LEU A 108 ? 0.2088 0.2419 0.2077 0.0041  -0.0159 0.0200  109 LEU A CA  
842  C C   . LEU A 108 ? 0.2115 0.2494 0.2105 0.0059  -0.0149 0.0195  109 LEU A C   
843  O O   . LEU A 108 ? 0.2003 0.2442 0.1980 0.0055  -0.0156 0.0200  109 LEU A O   
844  C CB  . LEU A 108 ? 0.2310 0.2634 0.2352 0.0050  -0.0157 0.0246  109 LEU A CB  
845  C CG  . LEU A 108 ? 0.2911 0.3311 0.2957 0.0062  -0.0163 0.0296  109 LEU A CG  
846  C CD1 . LEU A 108 ? 0.2736 0.3179 0.2751 0.0040  -0.0172 0.0294  109 LEU A CD1 
847  C CD2 . LEU A 108 ? 0.2996 0.3374 0.3088 0.0078  -0.0154 0.0355  109 LEU A CD2 
848  N N   . GLN A 109 ? 0.2124 0.2480 0.2135 0.0076  -0.0132 0.0179  110 GLN A N   
849  C CA  . GLN A 109 ? 0.2202 0.2614 0.2234 0.0088  -0.0120 0.0169  110 GLN A CA  
850  C C   . GLN A 109 ? 0.2160 0.2575 0.2146 0.0067  -0.0108 0.0137  110 GLN A C   
851  O O   . GLN A 109 ? 0.2207 0.2681 0.2209 0.0062  -0.0106 0.0131  110 GLN A O   
852  C CB  . GLN A 109 ? 0.1785 0.2172 0.1862 0.0114  -0.0097 0.0157  110 GLN A CB  
853  C CG  . GLN A 109 ? 0.1895 0.2279 0.2033 0.0145  -0.0105 0.0199  110 GLN A CG  
854  C CD  . GLN A 109 ? 0.2238 0.2568 0.2425 0.0174  -0.0077 0.0183  110 GLN A CD  
855  O OE1 . GLN A 109 ? 0.2247 0.2522 0.2406 0.0164  -0.0052 0.0135  110 GLN A OE1 
856  N NE2 . GLN A 109 ? 0.2070 0.2416 0.2328 0.0214  -0.0080 0.0226  110 GLN A NE2 
857  N N   . LEU A 110 ? 0.2002 0.2353 0.1930 0.0055  -0.0101 0.0117  111 LEU A N   
858  C CA  . LEU A 110 ? 0.1696 0.2041 0.1573 0.0040  -0.0088 0.0104  111 LEU A CA  
859  C C   . LEU A 110 ? 0.2030 0.2409 0.1903 0.0030  -0.0108 0.0118  111 LEU A C   
860  O O   . LEU A 110 ? 0.2085 0.2486 0.1962 0.0021  -0.0095 0.0110  111 LEU A O   
861  C CB  . LEU A 110 ? 0.1753 0.2033 0.1558 0.0038  -0.0084 0.0088  111 LEU A CB  
862  C CG  . LEU A 110 ? 0.2505 0.2748 0.2294 0.0048  -0.0054 0.0061  111 LEU A CG  
863  C CD1 . LEU A 110 ? 0.2466 0.2657 0.2166 0.0046  -0.0061 0.0040  111 LEU A CD1 
864  C CD2 . LEU A 110 ? 0.2536 0.2798 0.2334 0.0048  -0.0012 0.0055  111 LEU A CD2 
865  N N   . ALA A 111 ? 0.2100 0.2481 0.1974 0.0029  -0.0134 0.0136  112 ALA A N   
866  C CA  . ALA A 111 ? 0.1908 0.2323 0.1778 0.0022  -0.0147 0.0146  112 ALA A CA  
867  C C   . ALA A 111 ? 0.2297 0.2781 0.2200 0.0022  -0.0147 0.0148  112 ALA A C   
868  O O   . ALA A 111 ? 0.2447 0.2957 0.2342 0.0015  -0.0145 0.0138  112 ALA A O   
869  C CB  . ALA A 111 ? 0.1788 0.2203 0.1665 0.0018  -0.0169 0.0164  112 ALA A CB  
870  N N   . THR A 112 ? 0.2015 0.2534 0.1955 0.0033  -0.0150 0.0158  113 THR A N   
871  C CA  . THR A 112 ? 0.1801 0.2406 0.1766 0.0038  -0.0160 0.0160  113 THR A CA  
872  C C   . THR A 112 ? 0.1960 0.2605 0.1966 0.0038  -0.0150 0.0134  113 THR A C   
873  O O   . THR A 112 ? 0.1809 0.2542 0.1849 0.0048  -0.0167 0.0136  113 THR A O   
874  C CB  . THR A 112 ? 0.1782 0.2420 0.1761 0.0057  -0.0178 0.0206  113 THR A CB  
875  O OG1 . THR A 112 ? 0.2136 0.2736 0.2147 0.0075  -0.0173 0.0223  113 THR A OG1 
876  C CG2 . THR A 112 ? 0.1992 0.2602 0.1946 0.0048  -0.0181 0.0229  113 THR A CG2 
877  N N   . TYR A 113 ? 0.2028 0.2621 0.2032 0.0029  -0.0122 0.0111  114 TYR A N   
878  C CA  . TYR A 113 ? 0.2050 0.2679 0.2099 0.0017  -0.0100 0.0079  114 TYR A CA  
879  C C   . TYR A 113 ? 0.1803 0.2496 0.1920 0.0039  -0.0105 0.0083  114 TYR A C   
880  O O   . TYR A 113 ? 0.1910 0.2688 0.2088 0.0031  -0.0106 0.0058  114 TYR A O   
881  C CB  . TYR A 113 ? 0.2198 0.2885 0.2265 -0.0007 -0.0103 0.0047  114 TYR A CB  
882  C CG  . TYR A 113 ? 0.2530 0.3177 0.2544 -0.0018 -0.0106 0.0047  114 TYR A CG  
883  C CD1 . TYR A 113 ? 0.2360 0.2915 0.2335 -0.0027 -0.0078 0.0046  114 TYR A CD1 
884  C CD2 . TYR A 113 ? 0.2390 0.3096 0.2393 -0.0014 -0.0133 0.0048  114 TYR A CD2 
885  C CE1 . TYR A 113 ? 0.2463 0.2987 0.2404 -0.0028 -0.0080 0.0048  114 TYR A CE1 
886  C CE2 . TYR A 113 ? 0.2381 0.3054 0.2345 -0.0020 -0.0129 0.0044  114 TYR A CE2 
887  C CZ  . TYR A 113 ? 0.2736 0.3320 0.2678 -0.0025 -0.0104 0.0044  114 TYR A CZ  
888  O OH  . TYR A 113 ? 0.3022 0.3582 0.2940 -0.0023 -0.0101 0.0042  114 TYR A OH  
889  N N   . THR A 114 ? 0.2057 0.2713 0.2176 0.0066  -0.0107 0.0110  115 THR A N   
890  C CA  . THR A 114 ? 0.2098 0.2812 0.2291 0.0098  -0.0111 0.0120  115 THR A CA  
891  C C   . THR A 114 ? 0.2275 0.2932 0.2488 0.0110  -0.0072 0.0105  115 THR A C   
892  O O   . THR A 114 ? 0.2215 0.2887 0.2485 0.0146  -0.0072 0.0120  115 THR A O   
893  C CB  . THR A 114 ? 0.2502 0.3236 0.2702 0.0131  -0.0144 0.0170  115 THR A CB  
894  O OG1 . THR A 114 ? 0.2246 0.2873 0.2407 0.0135  -0.0136 0.0190  115 THR A OG1 
895  C CG2 . THR A 114 ? 0.2010 0.2820 0.2183 0.0124  -0.0179 0.0185  115 THR A CG2 
896  N N   . SER A 115 ? 0.1946 0.2541 0.2114 0.0086  -0.0036 0.0077  116 SER A N   
897  C CA  . SER A 115 ? 0.1863 0.2408 0.2034 0.0097  0.0006  0.0059  116 SER A CA  
898  C C   . SER A 115 ? 0.2113 0.2742 0.2387 0.0113  0.0029  0.0044  116 SER A C   
899  O O   . SER A 115 ? 0.2023 0.2628 0.2325 0.0138  0.0061  0.0033  116 SER A O   
900  C CB  . SER A 115 ? 0.2020 0.2494 0.2108 0.0070  0.0043  0.0040  116 SER A CB  
901  O OG  . SER A 115 ? 0.2164 0.2683 0.2284 0.0044  0.0071  0.0025  116 SER A OG  
902  N N   . GLY A 116 ? 0.1983 0.2715 0.2322 0.0099  0.0014  0.0036  117 GLY A N   
903  C CA  . GLY A 116 ? 0.1978 0.2813 0.2433 0.0109  0.0032  0.0016  117 GLY A CA  
904  C C   . GLY A 116 ? 0.1853 0.2689 0.2331 0.0074  0.0094  -0.0020 117 GLY A C   
905  O O   . GLY A 116 ? 0.1729 0.2665 0.2322 0.0074  0.0113  -0.0042 117 GLY A O   
906  N N   . ASN A 117 ? 0.1768 0.2499 0.2147 0.0045  0.0128  -0.0022 118 ASN A N   
907  C CA  . ASN A 117 ? 0.2294 0.3020 0.2690 0.0010  0.0194  -0.0045 118 ASN A CA  
908  C C   . ASN A 117 ? 0.2130 0.2752 0.2413 -0.0022 0.0212  -0.0033 118 ASN A C   
909  O O   . ASN A 117 ? 0.2129 0.2678 0.2346 -0.0028 0.0268  -0.0028 118 ASN A O   
910  C CB  . ASN A 117 ? 0.1923 0.2631 0.2333 0.0030  0.0256  -0.0056 118 ASN A CB  
911  C CG  . ASN A 117 ? 0.2271 0.3008 0.2737 -0.0007 0.0331  -0.0076 118 ASN A CG  
912  O OD1 . ASN A 117 ? 0.2175 0.2977 0.2721 -0.0045 0.0331  -0.0091 118 ASN A OD1 
913  N ND2 . ASN A 117 ? 0.1917 0.2603 0.2339 0.0002  0.0401  -0.0080 118 ASN A ND2 
914  N N   . LEU A 118 ? 0.2261 0.2880 0.2518 -0.0037 0.0168  -0.0026 119 LEU A N   
915  C CA  . LEU A 118 ? 0.2056 0.2585 0.2230 -0.0062 0.0187  -0.0014 119 LEU A CA  
916  C C   . LEU A 118 ? 0.2049 0.2626 0.2285 -0.0097 0.0172  -0.0037 119 LEU A C   
917  O O   . LEU A 118 ? 0.1898 0.2538 0.2158 -0.0090 0.0115  -0.0045 119 LEU A O   
918  C CB  . LEU A 118 ? 0.2107 0.2556 0.2164 -0.0039 0.0150  0.0015  119 LEU A CB  
919  C CG  . LEU A 118 ? 0.2511 0.2898 0.2487 -0.0013 0.0166  0.0025  119 LEU A CG  
920  C CD1 . LEU A 118 ? 0.2338 0.2672 0.2227 0.0004  0.0117  0.0044  119 LEU A CD1 
921  C CD2 . LEU A 118 ? 0.2081 0.2408 0.2000 -0.0025 0.0234  0.0032  119 LEU A CD2 
922  N N   . ALA A 119 ? 0.2056 0.2595 0.2312 -0.0135 0.0227  -0.0047 120 ALA A N   
923  C CA  . ALA A 119 ? 0.2430 0.3007 0.2761 -0.0177 0.0226  -0.0083 120 ALA A CA  
924  C C   . ALA A 119 ? 0.2242 0.2728 0.2494 -0.0178 0.0214  -0.0068 120 ALA A C   
925  O O   . ALA A 119 ? 0.2266 0.2678 0.2411 -0.0146 0.0198  -0.0028 120 ALA A O   
926  C CB  . ALA A 119 ? 0.2651 0.3230 0.3071 -0.0222 0.0302  -0.0105 120 ALA A CB  
927  N N   . LEU A 120 ? 0.2195 0.2692 0.2508 -0.0217 0.0222  -0.0108 121 LEU A N   
928  C CA  . LEU A 120 ? 0.2741 0.3160 0.2996 -0.0214 0.0212  -0.0101 121 LEU A CA  
929  C C   . LEU A 120 ? 0.2529 0.2807 0.2691 -0.0197 0.0258  -0.0044 121 LEU A C   
930  O O   . LEU A 120 ? 0.2425 0.2648 0.2503 -0.0164 0.0230  -0.0011 121 LEU A O   
931  C CB  . LEU A 120 ? 0.2371 0.2813 0.2717 -0.0263 0.0227  -0.0165 121 LEU A CB  
932  C CG  . LEU A 120 ? 0.2890 0.3251 0.3188 -0.0257 0.0223  -0.0166 121 LEU A CG  
933  C CD1 . LEU A 120 ? 0.3240 0.3653 0.3471 -0.0216 0.0152  -0.0156 121 LEU A CD1 
934  C CD2 . LEU A 120 ? 0.3356 0.3726 0.3752 -0.0311 0.0247  -0.0243 121 LEU A CD2 
935  N N   . GLN A 121 ? 0.2615 0.2840 0.2794 -0.0217 0.0328  -0.0028 122 GLN A N   
936  C CA  . GLN A 121 ? 0.2707 0.2803 0.2789 -0.0198 0.0376  0.0035  122 GLN A CA  
937  C C   . GLN A 121 ? 0.2691 0.2782 0.2724 -0.0185 0.0413  0.0067  122 GLN A C   
938  O O   . GLN A 121 ? 0.2621 0.2797 0.2730 -0.0202 0.0425  0.0036  122 GLN A O   
939  C CB  . GLN A 121 ? 0.2647 0.2650 0.2778 -0.0235 0.0448  0.0037  122 GLN A CB  
940  C CG  . GLN A 121 ? 0.2531 0.2541 0.2736 -0.0260 0.0426  -0.0018 122 GLN A CG  
941  C CD  . GLN A 121 ? 0.3151 0.3110 0.3273 -0.0214 0.0382  0.0009  122 GLN A CD  
942  O OE1 . GLN A 121 ? 0.3229 0.3150 0.3242 -0.0166 0.0362  0.0069  122 GLN A OE1 
943  N NE2 . GLN A 121 ? 0.3508 0.3473 0.3685 -0.0230 0.0367  -0.0042 122 GLN A NE2 
944  N N   . PHE A 122 ? 0.2768 0.2766 0.2673 -0.0151 0.0432  0.0128  123 PHE A N   
945  C CA  . PHE A 122 ? 0.3169 0.3144 0.3012 -0.0142 0.0487  0.0159  123 PHE A CA  
946  C C   . PHE A 122 ? 0.2922 0.2882 0.2858 -0.0191 0.0580  0.0154  123 PHE A C   
947  O O   . PHE A 122 ? 0.3058 0.2978 0.3071 -0.0227 0.0608  0.0145  123 PHE A O   
948  C CB  . PHE A 122 ? 0.3021 0.2898 0.2703 -0.0099 0.0495  0.0228  123 PHE A CB  
949  C CG  . PHE A 122 ? 0.3038 0.2940 0.2627 -0.0054 0.0414  0.0231  123 PHE A CG  
950  C CD1 . PHE A 122 ? 0.2997 0.2956 0.2555 -0.0040 0.0394  0.0207  123 PHE A CD1 
951  C CD2 . PHE A 122 ? 0.3022 0.2892 0.2566 -0.0027 0.0362  0.0254  123 PHE A CD2 
952  C CE1 . PHE A 122 ? 0.3124 0.3100 0.2609 -0.0007 0.0322  0.0202  123 PHE A CE1 
953  C CE2 . PHE A 122 ? 0.3142 0.3044 0.2617 0.0007  0.0288  0.0252  123 PHE A CE2 
954  C CZ  . PHE A 122 ? 0.2943 0.2895 0.2389 0.0014  0.0268  0.0224  123 PHE A CZ  
955  N N   . PRO A 123 ? 0.3234 0.3223 0.3171 -0.0197 0.0635  0.0157  124 PRO A N   
956  C CA  . PRO A 123 ? 0.3832 0.3791 0.3842 -0.0243 0.0739  0.0167  124 PRO A CA  
957  C C   . PRO A 123 ? 0.4343 0.4155 0.4268 -0.0240 0.0795  0.0239  124 PRO A C   
958  O O   . PRO A 123 ? 0.3843 0.3586 0.3619 -0.0189 0.0763  0.0292  124 PRO A O   
959  C CB  . PRO A 123 ? 0.3953 0.3954 0.3925 -0.0229 0.0786  0.0173  124 PRO A CB  
960  C CG  . PRO A 123 ? 0.3897 0.3976 0.3838 -0.0188 0.0698  0.0139  124 PRO A CG  
961  C CD  . PRO A 123 ? 0.3229 0.3268 0.3097 -0.0160 0.0612  0.0152  124 PRO A CD  
962  N N   . ASP A 124 ? 0.4095 0.3862 0.4126 -0.0294 0.0880  0.0240  125 ASP A N   
963  C CA  . ASP A 124 ? 0.4553 0.4166 0.4526 -0.0292 0.0942  0.0313  125 ASP A CA  
964  C C   . ASP A 124 ? 0.4663 0.4196 0.4446 -0.0241 0.0986  0.0408  125 ASP A C   
965  O O   . ASP A 124 ? 0.5097 0.4516 0.4771 -0.0203 0.0992  0.0483  125 ASP A O   
966  C CB  . ASP A 124 ? 0.4817 0.4392 0.4949 -0.0368 0.1042  0.0297  125 ASP A CB  
967  C CG  . ASP A 124 ? 0.5472 0.5079 0.5764 -0.0416 0.1002  0.0213  125 ASP A CG  
968  O OD1 . ASP A 124 ? 0.5040 0.4706 0.5319 -0.0388 0.0900  0.0171  125 ASP A OD1 
969  O OD2 . ASP A 124 ? 0.5943 0.5516 0.6378 -0.0484 0.1078  0.0187  125 ASP A OD2 
970  N N   . GLU A 125 ? 0.4882 0.4480 0.4623 -0.0236 0.1017  0.0405  126 GLU A N   
971  C CA  . GLU A 125 ? 0.5281 0.4818 0.4832 -0.0191 0.1065  0.0485  126 GLU A CA  
972  C C   . GLU A 125 ? 0.4842 0.4382 0.4217 -0.0119 0.0967  0.0505  126 GLU A C   
973  O O   . GLU A 125 ? 0.4805 0.4288 0.4002 -0.0074 0.0992  0.0577  126 GLU A O   
974  C CB  . GLU A 125 ? 0.5591 0.5207 0.5162 -0.0210 0.1134  0.0461  126 GLU A CB  
975  C CG  . GLU A 125 ? 0.6254 0.6019 0.5950 -0.0222 0.1069  0.0360  126 GLU A CG  
976  C CD  . GLU A 125 ? 0.6817 0.6651 0.6751 -0.0290 0.1082  0.0294  126 GLU A CD  
977  O OE1 . GLU A 125 ? 0.7380 0.7341 0.7434 -0.0307 0.1073  0.0228  126 GLU A OE1 
978  O OE2 . GLU A 125 ? 0.7419 0.7184 0.7422 -0.0325 0.1098  0.0305  126 GLU A OE2 
979  N N   . VAL A 126 ? 0.4318 0.3926 0.3737 -0.0107 0.0858  0.0445  127 VAL A N   
980  C CA  . VAL A 126 ? 0.4156 0.3779 0.3436 -0.0048 0.0764  0.0452  127 VAL A CA  
981  C C   . VAL A 126 ? 0.4269 0.3810 0.3506 -0.0019 0.0729  0.0506  127 VAL A C   
982  O O   . VAL A 126 ? 0.3956 0.3510 0.3296 -0.0031 0.0678  0.0471  127 VAL A O   
983  C CB  . VAL A 126 ? 0.3607 0.3340 0.2960 -0.0051 0.0676  0.0369  127 VAL A CB  
984  C CG1 . VAL A 126 ? 0.3834 0.3577 0.3064 0.0001  0.0583  0.0374  127 VAL A CG1 
985  C CG2 . VAL A 126 ? 0.3690 0.3499 0.3086 -0.0068 0.0714  0.0323  127 VAL A CG2 
986  N N   . LYS A 127 ? 0.4222 0.3684 0.3301 0.0026  0.0754  0.0593  128 LYS A N   
987  C CA  . LYS A 127 ? 0.4066 0.3439 0.3111 0.0062  0.0738  0.0660  128 LYS A CA  
988  C C   . LYS A 127 ? 0.4468 0.3853 0.3351 0.0134  0.0656  0.0702  128 LYS A C   
989  O O   . LYS A 127 ? 0.4503 0.3845 0.3388 0.0169  0.0617  0.0739  128 LYS A O   
990  C CB  . LYS A 127 ? 0.4639 0.3884 0.3667 0.0054  0.0854  0.0748  128 LYS A CB  
991  C CG  . LYS A 127 ? 0.4959 0.4183 0.4174 -0.0024 0.0938  0.0707  128 LYS A CG  
992  C CD  . LYS A 127 ? 0.5258 0.4343 0.4462 -0.0036 0.1061  0.0799  128 LYS A CD  
993  C CE  . LYS A 127 ? 0.5576 0.4657 0.4976 -0.0125 0.1149  0.0746  128 LYS A CE  
994  N NZ  . LYS A 127 ? 0.5566 0.4652 0.5140 -0.0163 0.1106  0.0670  128 LYS A NZ  
995  N N   . THR A 128 ? 0.3712 0.3158 0.2462 0.0158  0.0630  0.0692  129 THR A N   
996  C CA  . THR A 128 ? 0.3789 0.3260 0.2379 0.0223  0.0553  0.0726  129 THR A CA  
997  C C   . THR A 128 ? 0.3961 0.3544 0.2553 0.0220  0.0461  0.0635  129 THR A C   
998  O O   . THR A 128 ? 0.3692 0.3324 0.2375 0.0176  0.0471  0.0560  129 THR A O   
999  C CB  . THR A 128 ? 0.4464 0.3897 0.2856 0.0261  0.0609  0.0804  129 THR A CB  
1000 O OG1 . THR A 128 ? 0.4074 0.3570 0.2420 0.0238  0.0634  0.0743  129 THR A OG1 
1001 C CG2 . THR A 128 ? 0.4124 0.3432 0.2523 0.0253  0.0729  0.0900  129 THR A CG2 
1002 N N   . ASP A 129 ? 0.3718 0.3343 0.2217 0.0268  0.0371  0.0643  130 ASP A N   
1003 C CA  . ASP A 129 ? 0.3993 0.3715 0.2493 0.0262  0.0287  0.0557  130 ASP A CA  
1004 C C   . ASP A 129 ? 0.4059 0.3811 0.2484 0.0245  0.0323  0.0509  130 ASP A C   
1005 O O   . ASP A 129 ? 0.3767 0.3572 0.2272 0.0215  0.0300  0.0426  130 ASP A O   
1006 C CB  . ASP A 129 ? 0.4319 0.4087 0.2721 0.0314  0.0191  0.0576  130 ASP A CB  
1007 C CG  . ASP A 129 ? 0.5255 0.5021 0.3764 0.0330  0.0141  0.0599  130 ASP A CG  
1008 O OD1 . ASP A 129 ? 0.5465 0.5211 0.4127 0.0292  0.0163  0.0573  130 ASP A OD1 
1009 O OD2 . ASP A 129 ? 0.5773 0.5568 0.4213 0.0381  0.0078  0.0638  130 ASP A OD2 
1010 N N   . GLN A 130 ? 0.3735 0.3452 0.2002 0.0270  0.0383  0.0563  131 GLN A N   
1011 C CA  . GLN A 130 ? 0.3969 0.3712 0.2159 0.0257  0.0432  0.0516  131 GLN A CA  
1012 C C   . GLN A 130 ? 0.3859 0.3601 0.2212 0.0203  0.0502  0.0468  131 GLN A C   
1013 O O   . GLN A 130 ? 0.3490 0.3284 0.1880 0.0185  0.0497  0.0386  131 GLN A O   
1014 C CB  . GLN A 130 ? 0.4411 0.4111 0.2407 0.0291  0.0505  0.0595  131 GLN A CB  
1015 C CG  . GLN A 130 ? 0.4361 0.4090 0.2163 0.0352  0.0433  0.0634  131 GLN A CG  
1016 C CD  . GLN A 130 ? 0.4717 0.4416 0.2302 0.0388  0.0507  0.0706  131 GLN A CD  
1017 O OE1 . GLN A 130 ? 0.4490 0.4161 0.2060 0.0363  0.0614  0.0706  131 GLN A OE1 
1018 N NE2 . GLN A 130 ? 0.4691 0.4406 0.2104 0.0450  0.0450  0.0770  131 GLN A NE2 
1019 N N   . GLN A 131 ? 0.3581 0.3267 0.2042 0.0178  0.0566  0.0515  132 GLN A N   
1020 C CA  . GLN A 131 ? 0.3637 0.3338 0.2260 0.0125  0.0631  0.0470  132 GLN A CA  
1021 C C   . GLN A 131 ? 0.3127 0.2894 0.1909 0.0101  0.0557  0.0389  132 GLN A C   
1022 O O   . GLN A 131 ? 0.3012 0.2826 0.1901 0.0072  0.0585  0.0331  132 GLN A O   
1023 C CB  . GLN A 131 ? 0.3566 0.3194 0.2270 0.0099  0.0715  0.0534  132 GLN A CB  
1024 C CG  . GLN A 131 ? 0.3598 0.3153 0.2148 0.0120  0.0810  0.0624  132 GLN A CG  
1025 C CD  . GLN A 131 ? 0.4489 0.3941 0.3091 0.0107  0.0878  0.0707  132 GLN A CD  
1026 O OE1 . GLN A 131 ? 0.4114 0.3550 0.2876 0.0077  0.0860  0.0687  132 GLN A OE1 
1027 N NE2 . GLN A 131 ? 0.4244 0.3622 0.2708 0.0130  0.0961  0.0802  132 GLN A NE2 
1028 N N   . VAL A 132 ? 0.3125 0.2901 0.1924 0.0117  0.0466  0.0387  133 VAL A N   
1029 C CA  . VAL A 132 ? 0.2976 0.2814 0.1907 0.0098  0.0398  0.0319  133 VAL A CA  
1030 C C   . VAL A 132 ? 0.3252 0.3142 0.2145 0.0105  0.0365  0.0254  133 VAL A C   
1031 O O   . VAL A 132 ? 0.2979 0.2913 0.1987 0.0085  0.0356  0.0199  133 VAL A O   
1032 C CB  . VAL A 132 ? 0.3077 0.2915 0.2033 0.0113  0.0318  0.0335  133 VAL A CB  
1033 C CG1 . VAL A 132 ? 0.3213 0.3118 0.2265 0.0100  0.0245  0.0269  133 VAL A CG1 
1034 C CG2 . VAL A 132 ? 0.3465 0.3254 0.2510 0.0096  0.0353  0.0373  133 VAL A CG2 
1035 N N   . LEU A 133 ? 0.3098 0.2984 0.1831 0.0137  0.0342  0.0258  134 LEU A N   
1036 C CA  . LEU A 133 ? 0.2949 0.2874 0.1643 0.0141  0.0318  0.0186  134 LEU A CA  
1037 C C   . LEU A 133 ? 0.3139 0.3068 0.1861 0.0127  0.0406  0.0155  134 LEU A C   
1038 O O   . LEU A 133 ? 0.3291 0.3253 0.2102 0.0117  0.0400  0.0090  134 LEU A O   
1039 C CB  . LEU A 133 ? 0.3053 0.2981 0.1561 0.0176  0.0278  0.0189  134 LEU A CB  
1040 C CG  . LEU A 133 ? 0.3420 0.3380 0.1861 0.0179  0.0259  0.0105  134 LEU A CG  
1041 C CD1 . LEU A 133 ? 0.3239 0.3226 0.1828 0.0157  0.0202  0.0037  134 LEU A CD1 
1042 C CD2 . LEU A 133 ? 0.3780 0.3758 0.2032 0.0212  0.0206  0.0107  134 LEU A CD2 
1043 N N   . THR A 134 ? 0.3059 0.2955 0.1713 0.0129  0.0493  0.0206  135 THR A N   
1044 C CA  . THR A 134 ? 0.3092 0.3002 0.1791 0.0113  0.0587  0.0180  135 THR A CA  
1045 C C   . THR A 134 ? 0.3112 0.3061 0.2030 0.0080  0.0594  0.0150  135 THR A C   
1046 O O   . THR A 134 ? 0.3088 0.3081 0.2088 0.0077  0.0618  0.0093  135 THR A O   
1047 C CB  . THR A 134 ? 0.3248 0.3114 0.1857 0.0114  0.0686  0.0253  135 THR A CB  
1048 O OG1 . THR A 134 ? 0.3430 0.3273 0.1814 0.0153  0.0681  0.0281  135 THR A OG1 
1049 C CG2 . THR A 134 ? 0.3272 0.3163 0.1961 0.0091  0.0795  0.0229  135 THR A CG2 
1050 N N   . PHE A 135 ? 0.2832 0.2771 0.1848 0.0060  0.0572  0.0186  136 PHE A N   
1051 C CA  . PHE A 135 ? 0.2753 0.2743 0.1966 0.0030  0.0564  0.0154  136 PHE A CA  
1052 C C   . PHE A 135 ? 0.2771 0.2812 0.2048 0.0042  0.0495  0.0093  136 PHE A C   
1053 O O   . PHE A 135 ? 0.2512 0.2608 0.1912 0.0034  0.0515  0.0054  136 PHE A O   
1054 C CB  . PHE A 135 ? 0.2946 0.2913 0.2224 0.0011  0.0534  0.0190  136 PHE A CB  
1055 C CG  . PHE A 135 ? 0.2486 0.2519 0.1948 -0.0017 0.0508  0.0152  136 PHE A CG  
1056 C CD1 . PHE A 135 ? 0.2709 0.2783 0.2301 -0.0051 0.0573  0.0138  136 PHE A CD1 
1057 C CD2 . PHE A 135 ? 0.3043 0.3106 0.2547 -0.0009 0.0420  0.0131  136 PHE A CD2 
1058 C CE1 . PHE A 135 ? 0.2743 0.2895 0.2497 -0.0073 0.0540  0.0100  136 PHE A CE1 
1059 C CE2 . PHE A 135 ? 0.2876 0.3007 0.2529 -0.0029 0.0394  0.0100  136 PHE A CE2 
1060 C CZ  . PHE A 135 ? 0.2910 0.3089 0.2684 -0.0060 0.0449  0.0083  136 PHE A CZ  
1061 N N   . PHE A 136 ? 0.2603 0.2628 0.1808 0.0060  0.0415  0.0087  137 PHE A N   
1062 C CA  . PHE A 136 ? 0.2613 0.2673 0.1888 0.0067  0.0356  0.0036  137 PHE A CA  
1063 C C   . PHE A 136 ? 0.2633 0.2694 0.1867 0.0085  0.0385  -0.0017 137 PHE A C   
1064 O O   . PHE A 136 ? 0.2677 0.2766 0.2013 0.0090  0.0371  -0.0058 137 PHE A O   
1065 C CB  . PHE A 136 ? 0.2768 0.2815 0.2001 0.0074  0.0268  0.0042  137 PHE A CB  
1066 C CG  . PHE A 136 ? 0.2645 0.2706 0.1968 0.0059  0.0231  0.0073  137 PHE A CG  
1067 C CD1 . PHE A 136 ? 0.2684 0.2793 0.2150 0.0045  0.0223  0.0058  137 PHE A CD1 
1068 C CD2 . PHE A 136 ? 0.2986 0.3019 0.2248 0.0063  0.0206  0.0116  137 PHE A CD2 
1069 C CE1 . PHE A 136 ? 0.2723 0.2852 0.2259 0.0030  0.0192  0.0078  137 PHE A CE1 
1070 C CE2 . PHE A 136 ? 0.2832 0.2877 0.2177 0.0051  0.0179  0.0135  137 PHE A CE2 
1071 C CZ  . PHE A 136 ? 0.2903 0.2996 0.2378 0.0032  0.0173  0.0112  137 PHE A CZ  
1072 N N   . LYS A 137 ? 0.2716 0.2748 0.1804 0.0098  0.0429  -0.0018 138 LYS A N   
1073 C CA  . LYS A 137 ? 0.3019 0.3054 0.2070 0.0115  0.0466  -0.0080 138 LYS A CA  
1074 C C   . LYS A 137 ? 0.3420 0.3493 0.2595 0.0111  0.0546  -0.0094 138 LYS A C   
1075 O O   . LYS A 137 ? 0.3129 0.3219 0.2365 0.0126  0.0562  -0.0151 138 LYS A O   
1076 C CB  . LYS A 137 ? 0.3404 0.3409 0.2249 0.0131  0.0494  -0.0081 138 LYS A CB  
1077 C CG  . LYS A 137 ? 0.3214 0.3203 0.1938 0.0141  0.0407  -0.0088 138 LYS A CG  
1078 C CD  . LYS A 137 ? 0.4308 0.4288 0.2828 0.0163  0.0428  -0.0115 138 LYS A CD  
1079 C CE  . LYS A 137 ? 0.4475 0.4441 0.2883 0.0172  0.0515  -0.0049 138 LYS A CE  
1080 N NZ  . LYS A 137 ? 0.4488 0.4453 0.2672 0.0198  0.0538  -0.0073 138 LYS A NZ  
1081 N N   . ASP A 138 ? 0.3076 0.3165 0.2303 0.0090  0.0599  -0.0046 139 ASP A N   
1082 C CA  . ASP A 138 ? 0.3108 0.3252 0.2470 0.0080  0.0677  -0.0058 139 ASP A CA  
1083 C C   . ASP A 138 ? 0.2868 0.3076 0.2431 0.0070  0.0636  -0.0069 139 ASP A C   
1084 O O   . ASP A 138 ? 0.3164 0.3440 0.2864 0.0067  0.0688  -0.0087 139 ASP A O   
1085 C CB  . ASP A 138 ? 0.3410 0.3543 0.2748 0.0054  0.0758  -0.0003 139 ASP A CB  
1086 C CG  . ASP A 138 ? 0.4164 0.4245 0.3301 0.0069  0.0822  0.0017  139 ASP A CG  
1087 O OD1 . ASP A 138 ? 0.4461 0.4531 0.3484 0.0099  0.0809  -0.0027 139 ASP A OD1 
1088 O OD2 . ASP A 138 ? 0.4231 0.4284 0.3322 0.0052  0.0889  0.0077  139 ASP A OD2 
1089 N N   . TRP A 139 ? 0.2582 0.2783 0.2167 0.0068  0.0546  -0.0058 140 TRP A N   
1090 C CA  . TRP A 139 ? 0.2719 0.2985 0.2471 0.0061  0.0501  -0.0061 140 TRP A CA  
1091 C C   . TRP A 139 ? 0.2384 0.2697 0.2242 0.0091  0.0501  -0.0102 140 TRP A C   
1092 O O   . TRP A 139 ? 0.2384 0.2653 0.2180 0.0118  0.0497  -0.0134 140 TRP A O   
1093 C CB  . TRP A 139 ? 0.2505 0.2744 0.2227 0.0057  0.0411  -0.0040 140 TRP A CB  
1094 C CG  . TRP A 139 ? 0.2462 0.2765 0.2320 0.0051  0.0358  -0.0036 140 TRP A CG  
1095 C CD1 . TRP A 139 ? 0.2359 0.2700 0.2283 0.0023  0.0346  -0.0016 140 TRP A CD1 
1096 C CD2 . TRP A 139 ? 0.2059 0.2393 0.1993 0.0076  0.0309  -0.0051 140 TRP A CD2 
1097 N NE1 . TRP A 139 ? 0.2241 0.2647 0.2265 0.0030  0.0289  -0.0021 140 TRP A NE1 
1098 C CE2 . TRP A 139 ? 0.2037 0.2438 0.2070 0.0064  0.0267  -0.0034 140 TRP A CE2 
1099 C CE3 . TRP A 139 ? 0.2109 0.2416 0.2039 0.0108  0.0301  -0.0077 140 TRP A CE3 
1100 C CZ2 . TRP A 139 ? 0.1912 0.2358 0.2027 0.0088  0.0217  -0.0031 140 TRP A CZ2 
1101 C CZ3 . TRP A 139 ? 0.2052 0.2389 0.2078 0.0129  0.0255  -0.0072 140 TRP A CZ3 
1102 C CH2 . TRP A 139 ? 0.1952 0.2361 0.2063 0.0121  0.0212  -0.0043 140 TRP A CH2 
1103 N N   . LYS A 140 ? 0.2571 0.2974 0.2594 0.0088  0.0506  -0.0104 141 LYS A N   
1104 C CA  . LYS A 140 ? 0.2176 0.2638 0.2328 0.0124  0.0493  -0.0129 141 LYS A CA  
1105 C C   . LYS A 140 ? 0.2334 0.2867 0.2600 0.0122  0.0422  -0.0108 141 LYS A C   
1106 O O   . LYS A 140 ? 0.2547 0.3124 0.2847 0.0086  0.0411  -0.0091 141 LYS A O   
1107 C CB  . LYS A 140 ? 0.2248 0.2781 0.2503 0.0134  0.0577  -0.0155 141 LYS A CB  
1108 C CG  . LYS A 140 ? 0.3193 0.3662 0.3339 0.0152  0.0651  -0.0188 141 LYS A CG  
1109 C CD  . LYS A 140 ? 0.2931 0.3479 0.3206 0.0178  0.0727  -0.0221 141 LYS A CD  
1110 C CE  . LYS A 140 ? 0.3741 0.4225 0.3907 0.0205  0.0794  -0.0265 141 LYS A CE  
1111 N NZ  . LYS A 140 ? 0.4451 0.4895 0.4466 0.0173  0.0863  -0.0252 141 LYS A NZ  
1112 N N   . PRO A 141 ? 0.2028 0.2572 0.2353 0.0161  0.0375  -0.0108 142 PRO A N   
1113 C CA  . PRO A 141 ? 0.1935 0.2555 0.2353 0.0166  0.0306  -0.0081 142 PRO A CA  
1114 C C   . PRO A 141 ? 0.2464 0.3224 0.3043 0.0167  0.0322  -0.0089 142 PRO A C   
1115 O O   . PRO A 141 ? 0.2497 0.3299 0.3145 0.0178  0.0386  -0.0115 142 PRO A O   
1116 C CB  . PRO A 141 ? 0.2046 0.2624 0.2478 0.0213  0.0269  -0.0073 142 PRO A CB  
1117 C CG  . PRO A 141 ? 0.2050 0.2572 0.2468 0.0240  0.0331  -0.0111 142 PRO A CG  
1118 C CD  . PRO A 141 ? 0.2172 0.2650 0.2472 0.0202  0.0385  -0.0133 142 PRO A CD  
1119 N N   . LYS A 142 ? 0.2053 0.2898 0.2694 0.0156  0.0262  -0.0072 143 LYS A N   
1120 C CA  . LYS A 142 ? 0.2163 0.3166 0.2969 0.0163  0.0255  -0.0083 143 LYS A CA  
1121 C C   . LYS A 142 ? 0.2424 0.3499 0.3290 0.0209  0.0177  -0.0052 143 LYS A C   
1122 O O   . LYS A 142 ? 0.2215 0.3315 0.3155 0.0268  0.0176  -0.0042 143 LYS A O   
1123 C CB  . LYS A 142 ? 0.2112 0.3177 0.2949 0.0098  0.0264  -0.0103 143 LYS A CB  
1124 C CG  . LYS A 142 ? 0.2822 0.3883 0.3689 0.0066  0.0357  -0.0130 143 LYS A CG  
1125 C CD  . LYS A 142 ? 0.2846 0.3966 0.3775 -0.0002 0.0377  -0.0152 143 LYS A CD  
1126 C CE  . LYS A 142 ? 0.3080 0.4204 0.4059 -0.0030 0.0482  -0.0171 143 LYS A CE  
1127 N NZ  . LYS A 142 ? 0.3277 0.4465 0.4355 -0.0101 0.0513  -0.0197 143 LYS A NZ  
1128 N N   . ASN A 143 ? 0.2145 0.3248 0.2975 0.0187  0.0114  -0.0035 144 ASN A N   
1129 C CA  . ASN A 143 ? 0.2130 0.3297 0.2989 0.0230  0.0041  0.0004  144 ASN A CA  
1130 C C   . ASN A 143 ? 0.2123 0.3160 0.2900 0.0270  0.0031  0.0045  144 ASN A C   
1131 O O   . ASN A 143 ? 0.2353 0.3257 0.3020 0.0246  0.0056  0.0039  144 ASN A O   
1132 C CB  . ASN A 143 ? 0.2151 0.3373 0.2972 0.0192  -0.0014 0.0005  144 ASN A CB  
1133 C CG  . ASN A 143 ? 0.2278 0.3602 0.3175 0.0138  0.0002  -0.0048 144 ASN A CG  
1134 O OD1 . ASN A 143 ? 0.2544 0.3981 0.3573 0.0144  0.0021  -0.0074 144 ASN A OD1 
1135 N ND2 . ASN A 143 ? 0.3322 0.4606 0.4146 0.0084  -0.0002 -0.0065 144 ASN A ND2 
1136 N N   . SER A 144 ? 0.1962 0.3043 0.2797 0.0330  -0.0008 0.0088  145 SER A N   
1137 C CA  . SER A 144 ? 0.1920 0.2876 0.2699 0.0365  -0.0012 0.0129  145 SER A CA  
1138 C C   . SER A 144 ? 0.2092 0.2942 0.2733 0.0319  -0.0026 0.0136  145 SER A C   
1139 O O   . SER A 144 ? 0.1873 0.2776 0.2475 0.0293  -0.0067 0.0150  145 SER A O   
1140 C CB  . SER A 144 ? 0.2396 0.3421 0.3241 0.0430  -0.0062 0.0193  145 SER A CB  
1141 O OG  . SER A 144 ? 0.3428 0.4557 0.4412 0.0483  -0.0052 0.0190  145 SER A OG  
1142 N N   . ILE A 145 ? 0.1803 0.2513 0.2375 0.0308  0.0008  0.0120  146 ILE A N   
1143 C CA  . ILE A 145 ? 0.2236 0.2856 0.2690 0.0265  -0.0005 0.0122  146 ILE A CA  
1144 C C   . ILE A 145 ? 0.2152 0.2779 0.2590 0.0277  -0.0054 0.0179  146 ILE A C   
1145 O O   . ILE A 145 ? 0.1952 0.2559 0.2437 0.0322  -0.0062 0.0222  146 ILE A O   
1146 C CB  . ILE A 145 ? 0.2179 0.2665 0.2574 0.0259  0.0033  0.0091  146 ILE A CB  
1147 C CG1 . ILE A 145 ? 0.2625 0.3107 0.2999 0.0240  0.0085  0.0038  146 ILE A CG1 
1148 C CG2 . ILE A 145 ? 0.2195 0.2600 0.2490 0.0224  0.0008  0.0100  146 ILE A CG2 
1149 C CD1 . ILE A 145 ? 0.2397 0.2768 0.2715 0.0243  0.0124  -0.0002 146 ILE A CD1 
1150 N N   . GLY A 146 ? 0.1929 0.2583 0.2303 0.0239  -0.0082 0.0183  147 GLY A N   
1151 C CA  . GLY A 146 ? 0.2292 0.2956 0.2635 0.0243  -0.0120 0.0234  147 GLY A CA  
1152 C C   . GLY A 146 ? 0.2217 0.3019 0.2597 0.0265  -0.0160 0.0264  147 GLY A C   
1153 O O   . GLY A 146 ? 0.2278 0.3102 0.2614 0.0265  -0.0189 0.0305  147 GLY A O   
1154 N N   . GLU A 147 ? 0.1799 0.2706 0.2259 0.0283  -0.0162 0.0243  148 GLU A N   
1155 C CA  . GLU A 147 ? 0.1883 0.2938 0.2388 0.0314  -0.0209 0.0272  148 GLU A CA  
1156 C C   . GLU A 147 ? 0.1876 0.3043 0.2369 0.0271  -0.0233 0.0225  148 GLU A C   
1157 O O   . GLU A 147 ? 0.1933 0.3220 0.2427 0.0288  -0.0281 0.0244  148 GLU A O   
1158 C CB  . GLU A 147 ? 0.2480 0.3608 0.3104 0.0371  -0.0208 0.0282  148 GLU A CB  
1159 C CG  . GLU A 147 ? 0.2809 0.3827 0.3456 0.0426  -0.0187 0.0336  148 GLU A CG  
1160 C CD  . GLU A 147 ? 0.4082 0.5188 0.4851 0.0500  -0.0196 0.0367  148 GLU A CD  
1161 O OE1 . GLU A 147 ? 0.4564 0.5578 0.5368 0.0552  -0.0176 0.0411  148 GLU A OE1 
1162 O OE2 . GLU A 147 ? 0.4474 0.5744 0.5313 0.0509  -0.0225 0.0345  148 GLU A OE2 
1163 N N   . TYR A 148 ? 0.1899 0.3027 0.2378 0.0217  -0.0200 0.0164  149 TYR A N   
1164 C CA  . TYR A 148 ? 0.1816 0.3033 0.2302 0.0171  -0.0213 0.0110  149 TYR A CA  
1165 C C   . TYR A 148 ? 0.1886 0.3001 0.2283 0.0120  -0.0189 0.0085  149 TYR A C   
1166 O O   . TYR A 148 ? 0.2080 0.3080 0.2447 0.0105  -0.0146 0.0079  149 TYR A O   
1167 C CB  . TYR A 148 ? 0.2049 0.3342 0.2644 0.0156  -0.0188 0.0059  149 TYR A CB  
1168 C CG  . TYR A 148 ? 0.2222 0.3634 0.2923 0.0211  -0.0213 0.0080  149 TYR A CG  
1169 C CD1 . TYR A 148 ? 0.2568 0.3919 0.3309 0.0258  -0.0184 0.0110  149 TYR A CD1 
1170 C CD2 . TYR A 148 ? 0.2632 0.4222 0.3395 0.0223  -0.0269 0.0069  149 TYR A CD2 
1171 C CE1 . TYR A 148 ? 0.3054 0.4508 0.3902 0.0318  -0.0204 0.0135  149 TYR A CE1 
1172 C CE2 . TYR A 148 ? 0.2379 0.4089 0.3246 0.0285  -0.0298 0.0097  149 TYR A CE2 
1173 C CZ  . TYR A 148 ? 0.2704 0.4340 0.3616 0.0335  -0.0263 0.0134  149 TYR A CZ  
1174 O OH  . TYR A 148 ? 0.3248 0.4994 0.4276 0.0406  -0.0285 0.0165  149 TYR A OH  
1175 N N   . ARG A 149 ? 0.2026 0.3195 0.2385 0.0096  -0.0216 0.0067  150 ARG A N   
1176 C CA  . ARG A 149 ? 0.2245 0.3334 0.2535 0.0053  -0.0196 0.0040  150 ARG A CA  
1177 C C   . ARG A 149 ? 0.2084 0.3189 0.2424 0.0006  -0.0166 -0.0025 150 ARG A C   
1178 O O   . ARG A 149 ? 0.2107 0.3334 0.2516 -0.0009 -0.0186 -0.0067 150 ARG A O   
1179 C CB  . ARG A 149 ? 0.1766 0.2901 0.1993 0.0052  -0.0231 0.0047  150 ARG A CB  
1180 C CG  . ARG A 149 ? 0.1973 0.3032 0.2141 0.0015  -0.0209 0.0019  150 ARG A CG  
1181 C CD  . ARG A 149 ? 0.1807 0.2929 0.1919 0.0017  -0.0239 0.0018  150 ARG A CD  
1182 N NE  . ARG A 149 ? 0.1680 0.2723 0.1737 -0.0005 -0.0216 0.0002  150 ARG A NE  
1183 C CZ  . ARG A 149 ? 0.2274 0.3308 0.2342 -0.0040 -0.0197 -0.0061 150 ARG A CZ  
1184 N NH1 . ARG A 149 ? 0.1882 0.2973 0.2017 -0.0067 -0.0195 -0.0118 150 ARG A NH1 
1185 N NH2 . ARG A 149 ? 0.1777 0.2746 0.1799 -0.0049 -0.0179 -0.0068 150 ARG A NH2 
1186 N N   . GLN A 150 ? 0.1891 0.2878 0.2200 -0.0019 -0.0119 -0.0032 151 GLN A N   
1187 C CA  . GLN A 150 ? 0.2141 0.3113 0.2484 -0.0068 -0.0082 -0.0084 151 GLN A CA  
1188 C C   . GLN A 150 ? 0.2101 0.2944 0.2356 -0.0081 -0.0057 -0.0074 151 GLN A C   
1189 O O   . GLN A 150 ? 0.2038 0.2783 0.2242 -0.0068 -0.0032 -0.0040 151 GLN A O   
1190 C CB  . GLN A 150 ? 0.2384 0.3354 0.2801 -0.0080 -0.0034 -0.0099 151 GLN A CB  
1191 C CG  . GLN A 150 ? 0.2341 0.3288 0.2802 -0.0135 0.0013  -0.0146 151 GLN A CG  
1192 C CD  . GLN A 150 ? 0.3182 0.4176 0.3749 -0.0154 0.0059  -0.0168 151 GLN A CD  
1193 O OE1 . GLN A 150 ? 0.3124 0.4095 0.3689 -0.0125 0.0082  -0.0139 151 GLN A OE1 
1194 N NE2 . GLN A 150 ? 0.3480 0.4542 0.4147 -0.0204 0.0075  -0.0226 151 GLN A NE2 
1195 N N   . TYR A 151 ? 0.2210 0.3061 0.2451 -0.0104 -0.0065 -0.0105 152 TYR A N   
1196 C CA  . TYR A 151 ? 0.2198 0.2938 0.2370 -0.0109 -0.0044 -0.0094 152 TYR A CA  
1197 C C   . TYR A 151 ? 0.1978 0.2610 0.2143 -0.0122 0.0012  -0.0082 152 TYR A C   
1198 O O   . TYR A 151 ? 0.2181 0.2824 0.2412 -0.0151 0.0048  -0.0111 152 TYR A O   
1199 C CB  . TYR A 151 ? 0.2466 0.3235 0.2652 -0.0136 -0.0048 -0.0147 152 TYR A CB  
1200 C CG  . TYR A 151 ? 0.2760 0.3435 0.2885 -0.0131 -0.0033 -0.0136 152 TYR A CG  
1201 C CD1 . TYR A 151 ? 0.2862 0.3527 0.2921 -0.0098 -0.0059 -0.0095 152 TYR A CD1 
1202 C CD2 . TYR A 151 ? 0.3436 0.4035 0.3583 -0.0158 0.0011  -0.0169 152 TYR A CD2 
1203 C CE1 . TYR A 151 ? 0.3099 0.3694 0.3117 -0.0090 -0.0047 -0.0087 152 TYR A CE1 
1204 C CE2 . TYR A 151 ? 0.3724 0.4239 0.3824 -0.0144 0.0025  -0.0156 152 TYR A CE2 
1205 C CZ  . TYR A 151 ? 0.3876 0.4398 0.3915 -0.0108 -0.0007 -0.0117 152 TYR A CZ  
1206 O OH  . TYR A 151 ? 0.3942 0.4399 0.3950 -0.0091 0.0005  -0.0106 152 TYR A OH  
1207 N N   . SER A 152 ? 0.2131 0.2668 0.2217 -0.0099 0.0019  -0.0039 153 SER A N   
1208 C CA  . SER A 152 ? 0.2234 0.2685 0.2291 -0.0099 0.0065  -0.0015 153 SER A CA  
1209 C C   . SER A 152 ? 0.2238 0.2592 0.2204 -0.0078 0.0067  0.0023  153 SER A C   
1210 O O   . SER A 152 ? 0.2057 0.2410 0.1974 -0.0052 0.0030  0.0047  153 SER A O   
1211 C CB  . SER A 152 ? 0.2179 0.2657 0.2240 -0.0079 0.0062  0.0000  153 SER A CB  
1212 O OG  . SER A 152 ? 0.2168 0.2563 0.2170 -0.0071 0.0102  0.0024  153 SER A OG  
1213 N N   . ASN A 153 ? 0.1818 0.2091 0.1767 -0.0088 0.0111  0.0032  154 ASN A N   
1214 C CA  . ASN A 153 ? 0.2067 0.2253 0.1931 -0.0060 0.0113  0.0075  154 ASN A CA  
1215 C C   . ASN A 153 ? 0.2245 0.2402 0.2032 -0.0037 0.0113  0.0108  154 ASN A C   
1216 O O   . ASN A 153 ? 0.2332 0.2476 0.2056 -0.0009 0.0076  0.0132  154 ASN A O   
1217 C CB  . ASN A 153 ? 0.2054 0.2155 0.1927 -0.0073 0.0166  0.0083  154 ASN A CB  
1218 C CG  . ASN A 153 ? 0.2719 0.2834 0.2651 -0.0088 0.0160  0.0044  154 ASN A CG  
1219 O OD1 . ASN A 153 ? 0.2647 0.2797 0.2566 -0.0069 0.0116  0.0040  154 ASN A OD1 
1220 N ND2 . ASN A 153 ? 0.3336 0.3425 0.3338 -0.0126 0.0207  0.0011  154 ASN A ND2 
1221 N N   . PRO A 154 ? 0.2304 0.2459 0.2097 -0.0048 0.0153  0.0105  155 PRO A N   
1222 C CA  . PRO A 154 ? 0.2199 0.2336 0.1914 -0.0025 0.0152  0.0123  155 PRO A CA  
1223 C C   . PRO A 154 ? 0.2187 0.2373 0.1900 -0.0009 0.0094  0.0111  155 PRO A C   
1224 O O   . PRO A 154 ? 0.2581 0.2741 0.2218 0.0012  0.0072  0.0122  155 PRO A O   
1225 C CB  . PRO A 154 ? 0.2584 0.2735 0.2340 -0.0045 0.0210  0.0108  155 PRO A CB  
1226 C CG  . PRO A 154 ? 0.2713 0.2850 0.2539 -0.0078 0.0255  0.0102  155 PRO A CG  
1227 C CD  . PRO A 154 ? 0.2385 0.2551 0.2256 -0.0084 0.0209  0.0083  155 PRO A CD  
1228 N N   . SER A 155 ? 0.1864 0.2121 0.1660 -0.0018 0.0069  0.0087  156 SER A N   
1229 C CA  . SER A 155 ? 0.1793 0.2086 0.1597 -0.0002 0.0023  0.0085  156 SER A CA  
1230 C C   . SER A 155 ? 0.2012 0.2286 0.1769 0.0009  -0.0019 0.0102  156 SER A C   
1231 O O   . SER A 155 ? 0.2007 0.2261 0.1723 0.0021  -0.0040 0.0105  156 SER A O   
1232 C CB  . SER A 155 ? 0.1707 0.2084 0.1601 -0.0009 0.0005  0.0069  156 SER A CB  
1233 O OG  . SER A 155 ? 0.1941 0.2340 0.1850 0.0011  -0.0025 0.0076  156 SER A OG  
1234 N N   . ILE A 156 ? 0.2343 0.2626 0.2113 0.0004  -0.0028 0.0106  157 ILE A N   
1235 C CA  . ILE A 156 ? 0.2358 0.2638 0.2101 0.0017  -0.0065 0.0122  157 ILE A CA  
1236 C C   . ILE A 156 ? 0.2266 0.2489 0.1934 0.0033  -0.0063 0.0142  157 ILE A C   
1237 O O   . ILE A 156 ? 0.2608 0.2838 0.2253 0.0046  -0.0099 0.0151  157 ILE A O   
1238 C CB  . ILE A 156 ? 0.2741 0.3059 0.2525 0.0011  -0.0074 0.0117  157 ILE A CB  
1239 C CG1 . ILE A 156 ? 0.2935 0.3272 0.2712 0.0023  -0.0110 0.0131  157 ILE A CG1 
1240 C CG2 . ILE A 156 ? 0.2717 0.2993 0.2500 0.0007  -0.0040 0.0113  157 ILE A CG2 
1241 C CD1 . ILE A 156 ? 0.2870 0.3269 0.2690 0.0018  -0.0121 0.0124  157 ILE A CD1 
1242 N N   . GLY A 157 ? 0.2410 0.2582 0.2042 0.0034  -0.0021 0.0152  158 GLY A N   
1243 C CA  . GLY A 157 ? 0.2370 0.2493 0.1914 0.0058  -0.0020 0.0180  158 GLY A CA  
1244 C C   . GLY A 157 ? 0.2631 0.2759 0.2114 0.0066  -0.0044 0.0170  158 GLY A C   
1245 O O   . GLY A 157 ? 0.2638 0.2769 0.2066 0.0085  -0.0080 0.0180  158 GLY A O   
1246 N N   . LEU A 158 ? 0.2345 0.2482 0.1846 0.0053  -0.0024 0.0144  159 LEU A N   
1247 C CA  . LEU A 158 ? 0.2437 0.2574 0.1892 0.0058  -0.0042 0.0121  159 LEU A CA  
1248 C C   . LEU A 158 ? 0.2523 0.2693 0.2017 0.0055  -0.0097 0.0107  159 LEU A C   
1249 O O   . LEU A 158 ? 0.2547 0.2717 0.1993 0.0060  -0.0130 0.0092  159 LEU A O   
1250 C CB  . LEU A 158 ? 0.2092 0.2230 0.1580 0.0050  -0.0003 0.0095  159 LEU A CB  
1251 C CG  . LEU A 158 ? 0.2386 0.2513 0.1837 0.0056  -0.0010 0.0059  159 LEU A CG  
1252 C CD1 . LEU A 158 ? 0.2803 0.2901 0.2124 0.0070  -0.0013 0.0059  159 LEU A CD1 
1253 C CD2 . LEU A 158 ? 0.2456 0.2586 0.1952 0.0055  0.0038  0.0036  159 LEU A CD2 
1254 N N   . PHE A 159 ? 0.2179 0.2384 0.1761 0.0044  -0.0108 0.0110  160 PHE A N   
1255 C CA  . PHE A 159 ? 0.2220 0.2456 0.1845 0.0038  -0.0150 0.0106  160 PHE A CA  
1256 C C   . PHE A 159 ? 0.2424 0.2671 0.2013 0.0047  -0.0184 0.0118  160 PHE A C   
1257 O O   . PHE A 159 ? 0.2313 0.2575 0.1899 0.0043  -0.0220 0.0101  160 PHE A O   
1258 C CB  . PHE A 159 ? 0.2267 0.2543 0.1971 0.0029  -0.0150 0.0118  160 PHE A CB  
1259 C CG  . PHE A 159 ? 0.2314 0.2624 0.2063 0.0021  -0.0181 0.0125  160 PHE A CG  
1260 C CD1 . PHE A 159 ? 0.2132 0.2433 0.1914 0.0012  -0.0191 0.0117  160 PHE A CD1 
1261 C CD2 . PHE A 159 ? 0.2209 0.2553 0.1976 0.0023  -0.0194 0.0141  160 PHE A CD2 
1262 C CE1 . PHE A 159 ? 0.2407 0.2734 0.2240 0.0000  -0.0211 0.0128  160 PHE A CE1 
1263 C CE2 . PHE A 159 ? 0.1911 0.2293 0.1727 0.0013  -0.0214 0.0150  160 PHE A CE2 
1264 C CZ  . PHE A 159 ? 0.2259 0.2632 0.2108 -0.0001 -0.0222 0.0146  160 PHE A CZ  
1265 N N   . GLY A 160 ? 0.2297 0.2539 0.1869 0.0061  -0.0174 0.0143  161 GLY A N   
1266 C CA  . GLY A 160 ? 0.2321 0.2581 0.1872 0.0081  -0.0207 0.0160  161 GLY A CA  
1267 C C   . GLY A 160 ? 0.2529 0.2778 0.1990 0.0097  -0.0229 0.0156  161 GLY A C   
1268 O O   . GLY A 160 ? 0.2446 0.2738 0.1904 0.0105  -0.0277 0.0151  161 GLY A O   
1269 N N   . LYS A 161 ? 0.2568 0.2770 0.1952 0.0102  -0.0194 0.0158  162 LYS A N   
1270 C CA  . LYS A 161 ? 0.2716 0.2912 0.1993 0.0119  -0.0213 0.0150  162 LYS A CA  
1271 C C   . LYS A 161 ? 0.2694 0.2923 0.1985 0.0099  -0.0254 0.0095  162 LYS A C   
1272 O O   . LYS A 161 ? 0.2495 0.2762 0.1740 0.0108  -0.0303 0.0079  162 LYS A O   
1273 C CB  . LYS A 161 ? 0.3112 0.3253 0.2311 0.0124  -0.0154 0.0158  162 LYS A CB  
1274 C CG  . LYS A 161 ? 0.3849 0.3985 0.2925 0.0136  -0.0162 0.0136  162 LYS A CG  
1275 C CD  . LYS A 161 ? 0.3738 0.3890 0.2715 0.0173  -0.0196 0.0174  162 LYS A CD  
1276 C CE  . LYS A 161 ? 0.3675 0.3825 0.2501 0.0190  -0.0195 0.0157  162 LYS A CE  
1277 N NZ  . LYS A 161 ? 0.3986 0.4147 0.2699 0.0237  -0.0220 0.0215  162 LYS A NZ  
1278 N N   . VAL A 162 ? 0.2360 0.2579 0.1723 0.0072  -0.0236 0.0066  163 VAL A N   
1279 C CA  . VAL A 162 ? 0.2538 0.2769 0.1933 0.0049  -0.0264 0.0014  163 VAL A CA  
1280 C C   . VAL A 162 ? 0.2498 0.2786 0.1966 0.0036  -0.0316 0.0012  163 VAL A C   
1281 O O   . VAL A 162 ? 0.2451 0.2766 0.1913 0.0023  -0.0358 -0.0030 163 VAL A O   
1282 C CB  . VAL A 162 ? 0.2409 0.2607 0.1874 0.0032  -0.0227 -0.0002 163 VAL A CB  
1283 C CG1 . VAL A 162 ? 0.2470 0.2665 0.2000 0.0006  -0.0250 -0.0046 163 VAL A CG1 
1284 C CG2 . VAL A 162 ? 0.2733 0.2888 0.2132 0.0044  -0.0177 -0.0014 163 VAL A CG2 
1285 N N   . VAL A 163 ? 0.2276 0.2588 0.1816 0.0037  -0.0312 0.0051  164 VAL A N   
1286 C CA  . VAL A 163 ? 0.2146 0.2521 0.1762 0.0027  -0.0352 0.0052  164 VAL A CA  
1287 C C   . VAL A 163 ? 0.2354 0.2779 0.1920 0.0047  -0.0401 0.0047  164 VAL A C   
1288 O O   . VAL A 163 ? 0.2515 0.2997 0.2125 0.0029  -0.0447 0.0014  164 VAL A O   
1289 C CB  . VAL A 163 ? 0.2482 0.2877 0.2164 0.0032  -0.0331 0.0093  164 VAL A CB  
1290 C CG1 . VAL A 163 ? 0.2441 0.2911 0.2195 0.0031  -0.0366 0.0099  164 VAL A CG1 
1291 C CG2 . VAL A 163 ? 0.2040 0.2412 0.1779 0.0012  -0.0296 0.0097  164 VAL A CG2 
1292 N N   . ALA A 164 ? 0.2354 0.2761 0.1830 0.0085  -0.0393 0.0081  165 ALA A N   
1293 C CA  . ALA A 164 ? 0.2487 0.2945 0.1903 0.0117  -0.0443 0.0089  165 ALA A CA  
1294 C C   . ALA A 164 ? 0.2752 0.3228 0.2095 0.0105  -0.0480 0.0033  165 ALA A C   
1295 O O   . ALA A 164 ? 0.2571 0.3128 0.1925 0.0106  -0.0543 0.0006  165 ALA A O   
1296 C CB  . ALA A 164 ? 0.2664 0.3078 0.1992 0.0164  -0.0415 0.0148  165 ALA A CB  
1297 N N   . LEU A 165 ? 0.2763 0.3173 0.2034 0.0095  -0.0442 0.0008  166 LEU A N   
1298 C CA  . LEU A 165 ? 0.2849 0.3271 0.2050 0.0081  -0.0470 -0.0059 166 LEU A CA  
1299 C C   . LEU A 165 ? 0.2908 0.3373 0.2220 0.0035  -0.0510 -0.0123 166 LEU A C   
1300 O O   . LEU A 165 ? 0.2695 0.3218 0.1981 0.0024  -0.0565 -0.0180 166 LEU A O   
1301 C CB  . LEU A 165 ? 0.2671 0.3011 0.1804 0.0076  -0.0409 -0.0080 166 LEU A CB  
1302 C CG  . LEU A 165 ? 0.3204 0.3504 0.2202 0.0115  -0.0367 -0.0033 166 LEU A CG  
1303 C CD1 . LEU A 165 ? 0.2936 0.3166 0.1913 0.0105  -0.0296 -0.0051 166 LEU A CD1 
1304 C CD2 . LEU A 165 ? 0.3417 0.3763 0.2269 0.0144  -0.0412 -0.0042 166 LEU A CD2 
1305 N N   . SER A 166 ? 0.2577 0.3018 0.2016 0.0006  -0.0482 -0.0115 167 SER A N   
1306 C CA  . SER A 166 ? 0.2801 0.3266 0.2356 -0.0042 -0.0506 -0.0167 167 SER A CA  
1307 C C   . SER A 166 ? 0.2666 0.3239 0.2289 -0.0048 -0.0567 -0.0170 167 SER A C   
1308 O O   . SER A 166 ? 0.2772 0.3386 0.2477 -0.0092 -0.0600 -0.0228 167 SER A O   
1309 C CB  . SER A 166 ? 0.2409 0.2823 0.2072 -0.0064 -0.0456 -0.0139 167 SER A CB  
1310 O OG  . SER A 166 ? 0.2577 0.3037 0.2308 -0.0055 -0.0454 -0.0081 167 SER A OG  
1311 N N   . MET A 167 ? 0.2365 0.2987 0.1971 -0.0007 -0.0580 -0.0110 168 MET A N   
1312 C CA  . MET A 167 ? 0.2641 0.3379 0.2318 -0.0001 -0.0638 -0.0107 168 MET A CA  
1313 C C   . MET A 167 ? 0.3115 0.3922 0.2683 0.0041  -0.0700 -0.0113 168 MET A C   
1314 O O   . MET A 167 ? 0.2904 0.3820 0.2527 0.0060  -0.0754 -0.0103 168 MET A O   
1315 C CB  . MET A 167 ? 0.2859 0.3611 0.2609 0.0024  -0.0610 -0.0037 168 MET A CB  
1316 C CG  . MET A 167 ? 0.2948 0.3658 0.2805 -0.0016 -0.0557 -0.0029 168 MET A CG  
1317 S SD  . MET A 167 ? 0.4045 0.4751 0.3946 0.0015  -0.0510 0.0044  168 MET A SD  
1318 C CE  . MET A 167 ? 0.3546 0.4389 0.3554 0.0029  -0.0558 0.0049  168 MET A CE  
1319 N N   . ASN A 168 ? 0.3048 0.3799 0.2461 0.0062  -0.0691 -0.0123 169 ASN A N   
1320 C CA  A ASN A 168 ? 0.3194 0.4009 0.2475 0.0102  -0.0749 -0.0130 169 ASN A CA  
1321 C CA  B ASN A 168 ? 0.3134 0.3949 0.2415 0.0102  -0.0749 -0.0130 169 ASN A CA  
1322 C C   . ASN A 168 ? 0.3381 0.4242 0.2636 0.0170  -0.0768 -0.0043 169 ASN A C   
1323 O O   . ASN A 168 ? 0.3436 0.4402 0.2652 0.0205  -0.0840 -0.0042 169 ASN A O   
1324 C CB  A ASN A 168 ? 0.3535 0.4459 0.2856 0.0066  -0.0827 -0.0221 169 ASN A CB  
1325 C CB  B ASN A 168 ? 0.3458 0.4382 0.2781 0.0065  -0.0827 -0.0222 169 ASN A CB  
1326 C CG  A ASN A 168 ? 0.3357 0.4219 0.2703 0.0001  -0.0804 -0.0312 169 ASN A CG  
1327 C CG  B ASN A 168 ? 0.3507 0.4495 0.2664 0.0101  -0.0887 -0.0248 169 ASN A CG  
1328 O OD1 A ASN A 168 ? 0.3576 0.4334 0.2829 0.0003  -0.0749 -0.0318 169 ASN A OD1 
1329 O OD1 B ASN A 168 ? 0.4005 0.4922 0.2998 0.0135  -0.0853 -0.0222 169 ASN A OD1 
1330 N ND2 A ASN A 168 ? 0.3562 0.4486 0.3046 -0.0056 -0.0842 -0.0384 169 ASN A ND2 
1331 N ND2 B ASN A 168 ? 0.3953 0.5084 0.3152 0.0094  -0.0978 -0.0300 169 ASN A ND2 
1332 N N   . LYS A 169 ? 0.2904 0.3688 0.2183 0.0191  -0.0704 0.0028  170 LYS A N   
1333 C CA  . LYS A 169 ? 0.3104 0.3896 0.2364 0.0257  -0.0703 0.0114  170 LYS A CA  
1334 C C   . LYS A 169 ? 0.3216 0.3877 0.2410 0.0273  -0.0619 0.0170  170 LYS A C   
1335 O O   . LYS A 169 ? 0.2929 0.3518 0.2161 0.0230  -0.0563 0.0148  170 LYS A O   
1336 C CB  . LYS A 169 ? 0.3424 0.4281 0.2850 0.0260  -0.0713 0.0133  170 LYS A CB  
1337 C CG  . LYS A 169 ? 0.4114 0.5109 0.3660 0.0232  -0.0783 0.0078  170 LYS A CG  
1338 C CD  . LYS A 169 ? 0.4166 0.5201 0.3878 0.0229  -0.0764 0.0102  170 LYS A CD  
1339 C CE  . LYS A 169 ? 0.4883 0.6040 0.4745 0.0177  -0.0809 0.0039  170 LYS A CE  
1340 N NZ  . LYS A 169 ? 0.4454 0.5552 0.4362 0.0098  -0.0773 -0.0016 170 LYS A NZ  
1341 N N   . PRO A 170 ? 0.3047 0.3675 0.2156 0.0335  -0.0605 0.0246  171 PRO A N   
1342 C CA  . PRO A 170 ? 0.3340 0.3846 0.2427 0.0343  -0.0519 0.0298  171 PRO A CA  
1343 C C   . PRO A 170 ? 0.2937 0.3427 0.2175 0.0320  -0.0485 0.0298  171 PRO A C   
1344 O O   . PRO A 170 ? 0.2500 0.3069 0.1846 0.0323  -0.0522 0.0289  171 PRO A O   
1345 C CB  . PRO A 170 ? 0.3125 0.3608 0.2114 0.0417  -0.0518 0.0384  171 PRO A CB  
1346 C CG  . PRO A 170 ? 0.3555 0.4167 0.2527 0.0457  -0.0613 0.0382  171 PRO A CG  
1347 C CD  . PRO A 170 ? 0.3621 0.4319 0.2635 0.0399  -0.0666 0.0285  171 PRO A CD  
1348 N N   . PHE A 171 ? 0.2646 0.3042 0.1890 0.0296  -0.0413 0.0304  172 PHE A N   
1349 C CA  . PHE A 171 ? 0.2693 0.3079 0.2062 0.0270  -0.0380 0.0294  172 PHE A CA  
1350 C C   . PHE A 171 ? 0.2801 0.3211 0.2240 0.0313  -0.0387 0.0334  172 PHE A C   
1351 O O   . PHE A 171 ? 0.2560 0.3023 0.2111 0.0298  -0.0394 0.0313  172 PHE A O   
1352 C CB  . PHE A 171 ? 0.2586 0.2877 0.1942 0.0245  -0.0307 0.0297  172 PHE A CB  
1353 C CG  . PHE A 171 ? 0.2590 0.2879 0.2057 0.0219  -0.0276 0.0281  172 PHE A CG  
1354 C CD1 . PHE A 171 ? 0.2586 0.2914 0.2119 0.0176  -0.0284 0.0238  172 PHE A CD1 
1355 C CD2 . PHE A 171 ? 0.2697 0.2942 0.2199 0.0240  -0.0238 0.0310  172 PHE A CD2 
1356 C CE1 . PHE A 171 ? 0.2527 0.2863 0.2143 0.0156  -0.0258 0.0228  172 PHE A CE1 
1357 C CE2 . PHE A 171 ? 0.2709 0.2963 0.2301 0.0215  -0.0212 0.0286  172 PHE A CE2 
1358 C CZ  . PHE A 171 ? 0.2240 0.2544 0.1881 0.0175  -0.0224 0.0247  172 PHE A CZ  
1359 N N   . ASP A 172 ? 0.2628 0.2995 0.2003 0.0370  -0.0378 0.0395  173 ASP A N   
1360 C CA  . ASP A 172 ? 0.2795 0.3176 0.2245 0.0418  -0.0379 0.0433  173 ASP A CA  
1361 C C   . ASP A 172 ? 0.3104 0.3622 0.2635 0.0432  -0.0451 0.0413  173 ASP A C   
1362 O O   . ASP A 172 ? 0.2721 0.3280 0.2367 0.0444  -0.0447 0.0410  173 ASP A O   
1363 C CB  . ASP A 172 ? 0.3454 0.3762 0.2818 0.0485  -0.0360 0.0512  173 ASP A CB  
1364 C CG  . ASP A 172 ? 0.4098 0.4471 0.3353 0.0529  -0.0427 0.0541  173 ASP A CG  
1365 O OD1 . ASP A 172 ? 0.4476 0.4850 0.3629 0.0500  -0.0437 0.0517  173 ASP A OD1 
1366 O OD2 . ASP A 172 ? 0.4817 0.5249 0.4088 0.0594  -0.0472 0.0584  173 ASP A OD2 
1367 N N   . GLN A 173 ? 0.3042 0.3637 0.2521 0.0428  -0.0515 0.0392  174 GLN A N   
1368 C CA  A GLN A 173 ? 0.3019 0.3757 0.2588 0.0431  -0.0587 0.0363  174 GLN A CA  
1369 C CA  B GLN A 173 ? 0.2977 0.3715 0.2547 0.0431  -0.0587 0.0363  174 GLN A CA  
1370 C C   . GLN A 173 ? 0.2725 0.3506 0.2411 0.0360  -0.0580 0.0299  174 GLN A C   
1371 O O   . GLN A 173 ? 0.2768 0.3651 0.2577 0.0360  -0.0607 0.0284  174 GLN A O   
1372 C CB  A GLN A 173 ? 0.3120 0.3930 0.2593 0.0443  -0.0660 0.0350  174 GLN A CB  
1373 C CB  B GLN A 173 ? 0.3129 0.3943 0.2605 0.0445  -0.0662 0.0351  174 GLN A CB  
1374 C CG  A GLN A 173 ? 0.3475 0.4274 0.2840 0.0526  -0.0680 0.0426  174 GLN A CG  
1375 C CG  B GLN A 173 ? 0.3476 0.4270 0.2833 0.0527  -0.0679 0.0427  174 GLN A CG  
1376 C CD  A GLN A 173 ? 0.3355 0.4244 0.2822 0.0590  -0.0719 0.0465  174 GLN A CD  
1377 C CD  B GLN A 173 ? 0.3467 0.4373 0.2735 0.0548  -0.0768 0.0411  174 GLN A CD  
1378 O OE1 A GLN A 173 ? 0.3936 0.4971 0.3439 0.0608  -0.0802 0.0446  174 GLN A OE1 
1379 O OE1 B GLN A 173 ? 0.3277 0.4287 0.2600 0.0500  -0.0823 0.0335  174 GLN A OE1 
1380 N NE2 A GLN A 173 ? 0.3792 0.4602 0.3316 0.0626  -0.0659 0.0515  174 GLN A NE2 
1381 N NE2 B GLN A 173 ? 0.3983 0.4868 0.3113 0.0619  -0.0781 0.0483  174 GLN A NE2 
1382 N N   . VAL A 174 ? 0.2244 0.2955 0.1897 0.0304  -0.0541 0.0266  175 VAL A N   
1383 C CA  . VAL A 174 ? 0.2595 0.3333 0.2355 0.0245  -0.0525 0.0222  175 VAL A CA  
1384 C C   . VAL A 174 ? 0.2555 0.3305 0.2416 0.0258  -0.0488 0.0242  175 VAL A C   
1385 O O   . VAL A 174 ? 0.2201 0.3037 0.2176 0.0240  -0.0500 0.0223  175 VAL A O   
1386 C CB  . VAL A 174 ? 0.2598 0.3247 0.2306 0.0198  -0.0483 0.0198  175 VAL A CB  
1387 C CG1 . VAL A 174 ? 0.2396 0.3064 0.2210 0.0148  -0.0459 0.0172  175 VAL A CG1 
1388 C CG2 . VAL A 174 ? 0.3051 0.3700 0.2674 0.0181  -0.0518 0.0162  175 VAL A CG2 
1389 N N   . LEU A 175 ? 0.2471 0.3136 0.2294 0.0290  -0.0439 0.0277  176 LEU A N   
1390 C CA  . LEU A 175 ? 0.2258 0.2928 0.2170 0.0303  -0.0400 0.0284  176 LEU A CA  
1391 C C   . LEU A 175 ? 0.2625 0.3378 0.2609 0.0360  -0.0431 0.0307  176 LEU A C   
1392 O O   . LEU A 175 ? 0.2187 0.3022 0.2284 0.0355  -0.0428 0.0291  176 LEU A O   
1393 C CB  . LEU A 175 ? 0.2309 0.2860 0.2171 0.0314  -0.0337 0.0302  176 LEU A CB  
1394 C CG  . LEU A 175 ? 0.2273 0.2763 0.2093 0.0259  -0.0301 0.0275  176 LEU A CG  
1395 C CD1 . LEU A 175 ? 0.2263 0.2665 0.2074 0.0263  -0.0241 0.0280  176 LEU A CD1 
1396 C CD2 . LEU A 175 ? 0.2369 0.2924 0.2257 0.0211  -0.0304 0.0240  176 LEU A CD2 
1397 N N   . GLU A 176 ? 0.2510 0.3249 0.2434 0.0419  -0.0460 0.0350  177 GLU A N   
1398 C CA  . GLU A 176 ? 0.2723 0.3530 0.2721 0.0487  -0.0482 0.0382  177 GLU A CA  
1399 C C   . GLU A 176 ? 0.2510 0.3481 0.2598 0.0484  -0.0554 0.0358  177 GLU A C   
1400 O O   . GLU A 176 ? 0.2533 0.3593 0.2739 0.0521  -0.0562 0.0365  177 GLU A O   
1401 C CB  . GLU A 176 ? 0.3077 0.3813 0.2981 0.0560  -0.0488 0.0449  177 GLU A CB  
1402 C CG  . GLU A 176 ? 0.2698 0.3273 0.2555 0.0563  -0.0405 0.0471  177 GLU A CG  
1403 C CD  . GLU A 176 ? 0.3666 0.4148 0.3448 0.0636  -0.0390 0.0549  177 GLU A CD  
1404 O OE1 . GLU A 176 ? 0.3345 0.3884 0.3079 0.0692  -0.0449 0.0594  177 GLU A OE1 
1405 O OE2 . GLU A 176 ? 0.3174 0.3525 0.2946 0.0638  -0.0317 0.0564  177 GLU A OE2 
1406 N N   . LYS A 177 ? 0.2720 0.3737 0.2768 0.0438  -0.0602 0.0324  178 LYS A N   
1407 C CA  . LYS A 177 ? 0.2742 0.3920 0.2883 0.0428  -0.0674 0.0292  178 LYS A CA  
1408 C C   . LYS A 177 ? 0.2603 0.3834 0.2849 0.0346  -0.0660 0.0234  178 LYS A C   
1409 O O   . LYS A 177 ? 0.2420 0.3789 0.2794 0.0334  -0.0698 0.0209  178 LYS A O   
1410 C CB  . LYS A 177 ? 0.3110 0.4324 0.3144 0.0435  -0.0748 0.0285  178 LYS A CB  
1411 C CG  . LYS A 177 ? 0.3216 0.4414 0.3153 0.0527  -0.0775 0.0354  178 LYS A CG  
1412 C CD  . LYS A 177 ? 0.4350 0.5713 0.4306 0.0564  -0.0877 0.0347  178 LYS A CD  
1413 C CE  . LYS A 177 ? 0.4538 0.5893 0.4406 0.0669  -0.0903 0.0433  178 LYS A CE  
1414 N NZ  . LYS A 177 ? 0.5389 0.6688 0.5339 0.0731  -0.0846 0.0493  178 LYS A NZ  
1415 N N   . THR A 178 ? 0.2290 0.3418 0.2493 0.0291  -0.0606 0.0217  179 THR A N   
1416 C CA  . THR A 178 ? 0.2358 0.3520 0.2648 0.0218  -0.0588 0.0176  179 THR A CA  
1417 C C   . THR A 178 ? 0.2352 0.3470 0.2686 0.0205  -0.0511 0.0188  179 THR A C   
1418 O O   . THR A 178 ? 0.2081 0.3285 0.2537 0.0188  -0.0495 0.0179  179 THR A O   
1419 C CB  . THR A 178 ? 0.2414 0.3511 0.2624 0.0163  -0.0596 0.0142  179 THR A CB  
1420 O OG1 . THR A 178 ? 0.2935 0.4088 0.3101 0.0172  -0.0669 0.0119  179 THR A OG1 
1421 C CG2 . THR A 178 ? 0.2465 0.3583 0.2772 0.0091  -0.0573 0.0109  179 THR A CG2 
1422 N N   . ILE A 179 ? 0.1980 0.2978 0.2221 0.0211  -0.0463 0.0204  180 ILE A N   
1423 C CA  . ILE A 179 ? 0.1782 0.2746 0.2048 0.0187  -0.0399 0.0203  180 ILE A CA  
1424 C C   . ILE A 179 ? 0.2062 0.3059 0.2392 0.0233  -0.0366 0.0217  180 ILE A C   
1425 O O   . ILE A 179 ? 0.1988 0.3046 0.2400 0.0216  -0.0333 0.0207  180 ILE A O   
1426 C CB  . ILE A 179 ? 0.1738 0.2578 0.1893 0.0173  -0.0365 0.0206  180 ILE A CB  
1427 C CG1 . ILE A 179 ? 0.1771 0.2581 0.1878 0.0130  -0.0389 0.0187  180 ILE A CG1 
1428 C CG2 . ILE A 179 ? 0.1796 0.2618 0.1969 0.0154  -0.0307 0.0202  180 ILE A CG2 
1429 C CD1 . ILE A 179 ? 0.1882 0.2744 0.2071 0.0077  -0.0387 0.0169  180 ILE A CD1 
1430 N N   . PHE A 180 ? 0.1859 0.2817 0.2154 0.0294  -0.0370 0.0241  181 PHE A N   
1431 C CA  . PHE A 180 ? 0.2094 0.3071 0.2456 0.0343  -0.0334 0.0249  181 PHE A CA  
1432 C C   . PHE A 180 ? 0.2001 0.3125 0.2502 0.0356  -0.0355 0.0243  181 PHE A C   
1433 O O   . PHE A 180 ? 0.1875 0.3042 0.2452 0.0355  -0.0307 0.0229  181 PHE A O   
1434 C CB  . PHE A 180 ? 0.2266 0.3161 0.2574 0.0410  -0.0335 0.0284  181 PHE A CB  
1435 C CG  . PHE A 180 ? 0.2509 0.3257 0.2707 0.0398  -0.0294 0.0288  181 PHE A CG  
1436 C CD1 . PHE A 180 ? 0.2143 0.2851 0.2316 0.0343  -0.0252 0.0256  181 PHE A CD1 
1437 C CD2 . PHE A 180 ? 0.2794 0.3452 0.2920 0.0445  -0.0296 0.0329  181 PHE A CD2 
1438 C CE1 . PHE A 180 ? 0.2402 0.2991 0.2493 0.0330  -0.0216 0.0254  181 PHE A CE1 
1439 C CE2 . PHE A 180 ? 0.2754 0.3281 0.2796 0.0429  -0.0251 0.0332  181 PHE A CE2 
1440 C CZ  . PHE A 180 ? 0.2517 0.3015 0.2549 0.0369  -0.0213 0.0290  181 PHE A CZ  
1441 N N   . PRO A 181 ? 0.1943 0.3160 0.2485 0.0367  -0.0423 0.0248  182 PRO A N   
1442 C CA  . PRO A 181 ? 0.2174 0.3548 0.2872 0.0372  -0.0440 0.0236  182 PRO A CA  
1443 C C   . PRO A 181 ? 0.2309 0.3738 0.3079 0.0297  -0.0406 0.0207  182 PRO A C   
1444 O O   . PRO A 181 ? 0.2163 0.3689 0.3055 0.0302  -0.0373 0.0200  182 PRO A O   
1445 C CB  . PRO A 181 ? 0.2499 0.3957 0.3206 0.0386  -0.0530 0.0238  182 PRO A CB  
1446 C CG  . PRO A 181 ? 0.2606 0.3946 0.3159 0.0423  -0.0550 0.0269  182 PRO A CG  
1447 C CD  . PRO A 181 ? 0.2233 0.3427 0.2686 0.0382  -0.0487 0.0263  182 PRO A CD  
1448 N N   . ALA A 182 ? 0.2122 0.3489 0.2822 0.0232  -0.0407 0.0194  183 ALA A N   
1449 C CA  . ALA A 182 ? 0.2060 0.3461 0.2822 0.0165  -0.0368 0.0179  183 ALA A CA  
1450 C C   . ALA A 182 ? 0.2243 0.3617 0.2999 0.0170  -0.0288 0.0187  183 ALA A C   
1451 O O   . ALA A 182 ? 0.1923 0.3362 0.2757 0.0133  -0.0246 0.0185  183 ALA A O   
1452 C CB  . ALA A 182 ? 0.1949 0.3266 0.2630 0.0106  -0.0380 0.0170  183 ALA A CB  
1453 N N   . LEU A 183 ? 0.2376 0.3655 0.3040 0.0211  -0.0264 0.0194  184 LEU A N   
1454 C CA  . LEU A 183 ? 0.2382 0.3637 0.3028 0.0217  -0.0193 0.0187  184 LEU A CA  
1455 C C   . LEU A 183 ? 0.2523 0.3836 0.3251 0.0277  -0.0166 0.0181  184 LEU A C   
1456 O O   . LEU A 183 ? 0.2719 0.4016 0.3434 0.0288  -0.0105 0.0165  184 LEU A O   
1457 C CB  . LEU A 183 ? 0.1862 0.2983 0.2374 0.0219  -0.0177 0.0185  184 LEU A CB  
1458 C CG  . LEU A 183 ? 0.2251 0.3307 0.2679 0.0166  -0.0189 0.0189  184 LEU A CG  
1459 C CD1 . LEU A 183 ? 0.2319 0.3256 0.2637 0.0179  -0.0186 0.0185  184 LEU A CD1 
1460 C CD2 . LEU A 183 ? 0.2245 0.3333 0.2679 0.0122  -0.0145 0.0190  184 LEU A CD2 
1461 N N   . GLY A 184 ? 0.2529 0.3913 0.3340 0.0320  -0.0210 0.0191  185 GLY A N   
1462 C CA  . GLY A 184 ? 0.2772 0.4215 0.3677 0.0386  -0.0186 0.0189  185 GLY A CA  
1463 C C   . GLY A 184 ? 0.2548 0.3872 0.3385 0.0447  -0.0163 0.0193  185 GLY A C   
1464 O O   . GLY A 184 ? 0.3105 0.4445 0.4005 0.0496  -0.0117 0.0180  185 GLY A O   
1465 N N   . LEU A 185 ? 0.2524 0.3724 0.3240 0.0443  -0.0188 0.0208  186 LEU A N   
1466 C CA  . LEU A 185 ? 0.2399 0.3471 0.3055 0.0492  -0.0160 0.0214  186 LEU A CA  
1467 C C   . LEU A 185 ? 0.3352 0.4426 0.4035 0.0566  -0.0207 0.0258  186 LEU A C   
1468 O O   . LEU A 185 ? 0.3673 0.4769 0.4318 0.0561  -0.0273 0.0285  186 LEU A O   
1469 C CB  . LEU A 185 ? 0.2582 0.3524 0.3103 0.0448  -0.0152 0.0209  186 LEU A CB  
1470 C CG  . LEU A 185 ? 0.2419 0.3377 0.2906 0.0377  -0.0123 0.0176  186 LEU A CG  
1471 C CD1 . LEU A 185 ? 0.2642 0.3488 0.3011 0.0338  -0.0120 0.0172  186 LEU A CD1 
1472 C CD2 . LEU A 185 ? 0.2411 0.3407 0.2946 0.0382  -0.0057 0.0138  186 LEU A CD2 
1473 N N   . LYS A 186 ? 0.2596 0.3646 0.3340 0.0639  -0.0173 0.0265  187 LYS A N   
1474 C CA  . LYS A 186 ? 0.3037 0.4100 0.3817 0.0723  -0.0217 0.0318  187 LYS A CA  
1475 C C   . LYS A 186 ? 0.3098 0.3988 0.3799 0.0773  -0.0190 0.0353  187 LYS A C   
1476 O O   . LYS A 186 ? 0.2988 0.3870 0.3694 0.0847  -0.0227 0.0413  187 LYS A O   
1477 C CB  . LYS A 186 ? 0.3763 0.4958 0.4709 0.0784  -0.0207 0.0313  187 LYS A CB  
1478 C CG  . LYS A 186 ? 0.3660 0.5036 0.4704 0.0733  -0.0230 0.0284  187 LYS A CG  
1479 C CD  . LYS A 186 ? 0.4402 0.5828 0.5391 0.0683  -0.0313 0.0299  187 LYS A CD  
1480 C CE  . LYS A 186 ? 0.3861 0.5428 0.4934 0.0608  -0.0322 0.0263  187 LYS A CE  
1481 N NZ  . LYS A 186 ? 0.4331 0.5898 0.5326 0.0540  -0.0383 0.0260  187 LYS A NZ  
1482 N N   . HIS A 187 ? 0.2542 0.3297 0.3172 0.0733  -0.0128 0.0322  188 HIS A N   
1483 C CA  . HIS A 187 ? 0.3132 0.3714 0.3700 0.0769  -0.0092 0.0351  188 HIS A CA  
1484 C C   . HIS A 187 ? 0.3043 0.3516 0.3491 0.0691  -0.0070 0.0328  188 HIS A C   
1485 O O   . HIS A 187 ? 0.3034 0.3376 0.3459 0.0681  -0.0009 0.0304  188 HIS A O   
1486 C CB  . HIS A 187 ? 0.3048 0.3569 0.3705 0.0824  -0.0020 0.0327  188 HIS A CB  
1487 C CG  . HIS A 187 ? 0.3034 0.3648 0.3814 0.0917  -0.0040 0.0363  188 HIS A CG  
1488 N ND1 . HIS A 187 ? 0.3160 0.3903 0.4065 0.0931  -0.0020 0.0318  188 HIS A ND1 
1489 C CD2 . HIS A 187 ? 0.3123 0.3735 0.3922 0.1005  -0.0082 0.0443  188 HIS A CD2 
1490 C CE1 . HIS A 187 ? 0.3075 0.3895 0.4085 0.1023  -0.0048 0.0364  188 HIS A CE1 
1491 N NE2 . HIS A 187 ? 0.3125 0.3869 0.4071 0.1072  -0.0090 0.0442  188 HIS A NE2 
1492 N N   . SER A 188 ? 0.2532 0.3062 0.2915 0.0634  -0.0121 0.0330  189 SER A N   
1493 C CA  . SER A 188 ? 0.2640 0.3089 0.2916 0.0567  -0.0111 0.0315  189 SER A CA  
1494 C C   . SER A 188 ? 0.2726 0.3151 0.2913 0.0579  -0.0162 0.0373  189 SER A C   
1495 O O   . SER A 188 ? 0.2575 0.3101 0.2776 0.0604  -0.0225 0.0401  189 SER A O   
1496 C CB  . SER A 188 ? 0.2666 0.3200 0.2942 0.0492  -0.0117 0.0264  189 SER A CB  
1497 O OG  . SER A 188 ? 0.2468 0.3046 0.2820 0.0492  -0.0072 0.0216  189 SER A OG  
1498 N N   . TYR A 189 ? 0.2738 0.3036 0.2835 0.0560  -0.0133 0.0389  190 TYR A N   
1499 C CA  . TYR A 189 ? 0.2749 0.3001 0.2752 0.0588  -0.0164 0.0454  190 TYR A CA  
1500 C C   . TYR A 189 ? 0.3039 0.3205 0.2945 0.0528  -0.0139 0.0445  190 TYR A C   
1501 O O   . TYR A 189 ? 0.2989 0.3088 0.2908 0.0484  -0.0084 0.0403  190 TYR A O   
1502 C CB  . TYR A 189 ? 0.3115 0.3269 0.3122 0.0670  -0.0137 0.0521  190 TYR A CB  
1503 C CG  . TYR A 189 ? 0.3240 0.3469 0.3357 0.0743  -0.0153 0.0535  190 TYR A CG  
1504 C CD1 . TYR A 189 ? 0.3166 0.3521 0.3296 0.0793  -0.0230 0.0574  190 TYR A CD1 
1505 C CD2 . TYR A 189 ? 0.3134 0.3315 0.3349 0.0762  -0.0091 0.0502  190 TYR A CD2 
1506 C CE1 . TYR A 189 ? 0.3499 0.3939 0.3747 0.0862  -0.0246 0.0586  190 TYR A CE1 
1507 C CE2 . TYR A 189 ? 0.3439 0.3693 0.3765 0.0833  -0.0100 0.0512  190 TYR A CE2 
1508 C CZ  . TYR A 189 ? 0.3437 0.3823 0.3784 0.0885  -0.0178 0.0557  190 TYR A CZ  
1509 O OH  . TYR A 189 ? 0.3196 0.3670 0.3671 0.0958  -0.0186 0.0566  190 TYR A OH  
1510 N N   . VAL A 190 ? 0.2957 0.3135 0.2768 0.0530  -0.0180 0.0480  191 VAL A N   
1511 C CA  . VAL A 190 ? 0.3017 0.3090 0.2728 0.0502  -0.0145 0.0499  191 VAL A CA  
1512 C C   . VAL A 190 ? 0.3568 0.3532 0.3227 0.0566  -0.0115 0.0580  191 VAL A C   
1513 O O   . VAL A 190 ? 0.3431 0.3271 0.3063 0.0548  -0.0048 0.0594  191 VAL A O   
1514 C CB  . VAL A 190 ? 0.3420 0.3554 0.3047 0.0467  -0.0193 0.0488  191 VAL A CB  
1515 C CG1 . VAL A 190 ? 0.3487 0.3518 0.3012 0.0446  -0.0148 0.0510  191 VAL A CG1 
1516 C CG2 . VAL A 190 ? 0.3186 0.3403 0.2870 0.0403  -0.0209 0.0415  191 VAL A CG2 
1517 N N   . ASN A 191 ? 0.3225 0.3237 0.2873 0.0640  -0.0163 0.0638  192 ASN A N   
1518 C CA  . ASN A 191 ? 0.3667 0.3580 0.3273 0.0717  -0.0137 0.0729  192 ASN A CA  
1519 C C   . ASN A 191 ? 0.3738 0.3674 0.3461 0.0787  -0.0141 0.0746  192 ASN A C   
1520 O O   . ASN A 191 ? 0.3787 0.3863 0.3556 0.0821  -0.0211 0.0742  192 ASN A O   
1521 C CB  . ASN A 191 ? 0.3895 0.3850 0.3366 0.0759  -0.0194 0.0796  192 ASN A CB  
1522 C CG  . ASN A 191 ? 0.4581 0.4517 0.3936 0.0694  -0.0184 0.0774  192 ASN A CG  
1523 O OD1 . ASN A 191 ? 0.4763 0.4809 0.4081 0.0662  -0.0245 0.0730  192 ASN A OD1 
1524 N ND2 . ASN A 191 ? 0.4247 0.4041 0.3555 0.0672  -0.0102 0.0802  192 ASN A ND2 
1525 N N   . VAL A 192 ? 0.3754 0.3555 0.3536 0.0805  -0.0063 0.0758  193 VAL A N   
1526 C CA  . VAL A 192 ? 0.3917 0.3722 0.3818 0.0877  -0.0054 0.0770  193 VAL A CA  
1527 C C   . VAL A 192 ? 0.3948 0.3765 0.3812 0.0986  -0.0096 0.0879  193 VAL A C   
1528 O O   . VAL A 192 ? 0.4071 0.3767 0.3840 0.1018  -0.0065 0.0964  193 VAL A O   
1529 C CB  . VAL A 192 ? 0.4003 0.3644 0.3975 0.0865  0.0047  0.0745  193 VAL A CB  
1530 C CG1 . VAL A 192 ? 0.4048 0.3682 0.4144 0.0949  0.0063  0.0757  193 VAL A CG1 
1531 C CG2 . VAL A 192 ? 0.3639 0.3296 0.3646 0.0762  0.0077  0.0632  193 VAL A CG2 
1532 N N   . PRO A 193 ? 0.3757 0.3722 0.3695 0.1046  -0.0164 0.0885  194 PRO A N   
1533 C CA  . PRO A 193 ? 0.3970 0.3968 0.3878 0.1158  -0.0215 0.0991  194 PRO A CA  
1534 C C   . PRO A 193 ? 0.4577 0.4413 0.4538 0.1243  -0.0142 0.1066  194 PRO A C   
1535 O O   . PRO A 193 ? 0.4267 0.4006 0.4333 0.1225  -0.0065 0.1015  194 PRO A O   
1536 C CB  . PRO A 193 ? 0.4003 0.4217 0.4021 0.1186  -0.0299 0.0955  194 PRO A CB  
1537 C CG  . PRO A 193 ? 0.4727 0.5015 0.4801 0.1079  -0.0294 0.0837  194 PRO A CG  
1538 C CD  . PRO A 193 ? 0.4219 0.4337 0.4276 0.1013  -0.0197 0.0797  194 PRO A CD  
1539 N N   . LYS A 194 ? 0.4554 0.4366 0.4442 0.1343  -0.0170 0.1187  195 LYS A N   
1540 C CA  . LYS A 194 ? 0.4657 0.4296 0.4589 0.1433  -0.0097 0.1276  195 LYS A CA  
1541 C C   . LYS A 194 ? 0.4654 0.4329 0.4778 0.1492  -0.0083 0.1242  195 LYS A C   
1542 O O   . LYS A 194 ? 0.4949 0.4454 0.5156 0.1519  0.0010  0.1250  195 LYS A O   
1543 C CB  . LYS A 194 ? 0.5294 0.4922 0.5104 0.1540  -0.0139 0.1425  195 LYS A CB  
1544 C CG  . LYS A 194 ? 0.6151 0.5565 0.5988 0.1634  -0.0052 0.1539  195 LYS A CG  
1545 C CD  . LYS A 194 ? 0.6889 0.6068 0.6712 0.1548  0.0076  0.1510  195 LYS A CD  
1546 C CE  . LYS A 194 ? 0.6820 0.5768 0.6713 0.1627  0.0179  0.1599  195 LYS A CE  
1547 N NZ  . LYS A 194 ? 0.7712 0.6582 0.7473 0.1717  0.0177  0.1764  195 LYS A NZ  
1548 N N   . THR A 195 ? 0.4633 0.4530 0.4841 0.1509  -0.0168 0.1197  196 THR A N   
1549 C CA  . THR A 195 ? 0.4958 0.4907 0.5355 0.1562  -0.0150 0.1157  196 THR A CA  
1550 C C   . THR A 195 ? 0.4535 0.4414 0.5018 0.1471  -0.0065 0.1032  196 THR A C   
1551 O O   . THR A 195 ? 0.4616 0.4516 0.5251 0.1510  -0.0030 0.0989  196 THR A O   
1552 C CB  . THR A 195 ? 0.4554 0.4773 0.5028 0.1592  -0.0260 0.1135  196 THR A CB  
1553 O OG1 . THR A 195 ? 0.4969 0.5310 0.5412 0.1472  -0.0297 0.1035  196 THR A OG1 
1554 C CG2 . THR A 195 ? 0.4726 0.5035 0.5115 0.1689  -0.0354 0.1252  196 THR A CG2 
1555 N N   . GLN A 196 ? 0.4494 0.4296 0.4884 0.1355  -0.0029 0.0974  197 GLN A N   
1556 C CA  . GLN A 196 ? 0.4265 0.4009 0.4718 0.1266  0.0045  0.0856  197 GLN A CA  
1557 C C   . GLN A 196 ? 0.4474 0.3984 0.4880 0.1224  0.0142  0.0855  197 GLN A C   
1558 O O   . GLN A 196 ? 0.3903 0.3365 0.4348 0.1144  0.0200  0.0752  197 GLN A O   
1559 C CB  . GLN A 196 ? 0.3702 0.3593 0.4114 0.1158  -0.0003 0.0767  197 GLN A CB  
1560 C CG  . GLN A 196 ? 0.3802 0.3915 0.4303 0.1176  -0.0075 0.0737  197 GLN A CG  
1561 C CD  . GLN A 196 ? 0.3915 0.4060 0.4570 0.1193  -0.0024 0.0665  197 GLN A CD  
1562 O OE1 . GLN A 196 ? 0.3813 0.3847 0.4489 0.1147  0.0057  0.0597  197 GLN A OE1 
1563 N NE2 . GLN A 196 ? 0.3955 0.4264 0.4722 0.1258  -0.0070 0.0675  197 GLN A NE2 
1564 N N   . MET A 197 ? 0.4222 0.3592 0.4548 0.1274  0.0163  0.0966  198 MET A N   
1565 C CA  . MET A 197 ? 0.4758 0.3909 0.5047 0.1223  0.0260  0.0967  198 MET A CA  
1566 C C   . MET A 197 ? 0.4607 0.3618 0.5035 0.1229  0.0357  0.0903  198 MET A C   
1567 O O   . MET A 197 ? 0.4406 0.3297 0.4844 0.1143  0.0430  0.0830  198 MET A O   
1568 C CB  . MET A 197 ? 0.5168 0.4193 0.5351 0.1288  0.0273  0.1115  198 MET A CB  
1569 C CG  . MET A 197 ? 0.5914 0.5015 0.5928 0.1244  0.0214  0.1154  198 MET A CG  
1570 S SD  . MET A 197 ? 0.7663 0.6752 0.7629 0.1082  0.0248  0.1036  198 MET A SD  
1571 C CE  . MET A 197 ? 0.5925 0.5158 0.5714 0.1066  0.0154  0.1082  198 MET A CE  
1572 N N   . GLN A 198 ? 0.4546 0.3575 0.5090 0.1330  0.0359  0.0923  199 GLN A N   
1573 C CA  . GLN A 198 ? 0.4210 0.3107 0.4891 0.1340  0.0454  0.0851  199 GLN A CA  
1574 C C   . GLN A 198 ? 0.4324 0.3315 0.5059 0.1245  0.0466  0.0688  199 GLN A C   
1575 O O   . GLN A 198 ? 0.4376 0.3255 0.5204 0.1229  0.0549  0.0603  199 GLN A O   
1576 C CB  . GLN A 198 ? 0.5006 0.3907 0.5803 0.1483  0.0453  0.0916  199 GLN A CB  
1577 C CG  . GLN A 198 ? 0.5479 0.4636 0.6341 0.1523  0.0367  0.0885  199 GLN A CG  
1578 C CD  . GLN A 198 ? 0.6164 0.5501 0.6920 0.1540  0.0249  0.0967  199 GLN A CD  
1579 O OE1 . GLN A 198 ? 0.5781 0.5056 0.6398 0.1526  0.0229  0.1049  199 GLN A OE1 
1580 N NE2 . GLN A 198 ? 0.6341 0.5906 0.7167 0.1568  0.0173  0.0940  199 GLN A NE2 
1581 N N   . ASN A 199 ? 0.4053 0.3243 0.4732 0.1184  0.0388  0.0643  200 ASN A N   
1582 C CA  . ASN A 199 ? 0.3971 0.3258 0.4677 0.1092  0.0395  0.0504  200 ASN A CA  
1583 C C   . ASN A 199 ? 0.3827 0.3084 0.4434 0.0970  0.0402  0.0451  200 ASN A C   
1584 O O   . ASN A 199 ? 0.3845 0.3173 0.4462 0.0892  0.0410  0.0339  200 ASN A O   
1585 C CB  . ASN A 199 ? 0.3349 0.2878 0.4076 0.1103  0.0312  0.0488  200 ASN A CB  
1586 C CG  . ASN A 199 ? 0.4304 0.3896 0.5161 0.1213  0.0312  0.0510  200 ASN A CG  
1587 O OD1 . ASN A 199 ? 0.3933 0.3402 0.4884 0.1263  0.0389  0.0486  200 ASN A OD1 
1588 N ND2 . ASN A 199 ? 0.4148 0.3932 0.5023 0.1253  0.0228  0.0551  200 ASN A ND2 
1589 N N   . TYR A 200 ? 0.3773 0.2935 0.4286 0.0955  0.0401  0.0530  201 TYR A N   
1590 C CA  . TYR A 200 ? 0.4175 0.3334 0.4595 0.0848  0.0398  0.0494  201 TYR A CA  
1591 C C   . TYR A 200 ? 0.4537 0.3519 0.5000 0.0790  0.0494  0.0429  201 TYR A C   
1592 O O   . TYR A 200 ? 0.4543 0.3345 0.5020 0.0822  0.0557  0.0493  201 TYR A O   
1593 C CB  . TYR A 200 ? 0.4242 0.3398 0.4541 0.0865  0.0353  0.0609  201 TYR A CB  
1594 C CG  . TYR A 200 ? 0.4894 0.4064 0.5093 0.0767  0.0343  0.0587  201 TYR A CG  
1595 C CD1 . TYR A 200 ? 0.4432 0.3649 0.4649 0.0670  0.0355  0.0473  201 TYR A CD1 
1596 C CD2 . TYR A 200 ? 0.5178 0.4321 0.5261 0.0779  0.0323  0.0683  201 TYR A CD2 
1597 C CE1 . TYR A 200 ? 0.4537 0.3769 0.4675 0.0590  0.0346  0.0458  201 TYR A CE1 
1598 C CE2 . TYR A 200 ? 0.5438 0.4594 0.5438 0.0696  0.0320  0.0663  201 TYR A CE2 
1599 C CZ  . TYR A 200 ? 0.5379 0.4580 0.5414 0.0603  0.0332  0.0551  201 TYR A CZ  
1600 O OH  . TYR A 200 ? 0.5171 0.4391 0.5136 0.0529  0.0329  0.0534  201 TYR A OH  
1601 N N   . ALA A 201 ? 0.4356 0.3393 0.4843 0.0703  0.0507  0.0303  202 ALA A N   
1602 C CA  . ALA A 201 ? 0.4354 0.3252 0.4892 0.0637  0.0590  0.0218  202 ALA A CA  
1603 C C   . ALA A 201 ? 0.4814 0.3607 0.5291 0.0580  0.0616  0.0264  202 ALA A C   
1604 O O   . ALA A 201 ? 0.5029 0.3914 0.5412 0.0546  0.0562  0.0301  202 ALA A O   
1605 C CB  . ALA A 201 ? 0.3822 0.2836 0.4376 0.0556  0.0581  0.0074  202 ALA A CB  
1606 N N   . PHE A 202 ? 0.4570 0.3167 0.5109 0.0568  0.0707  0.0260  203 PHE A N   
1607 C CA  . PHE A 202 ? 0.5369 0.3870 0.5878 0.0493  0.0750  0.0275  203 PHE A CA  
1608 C C   . PHE A 202 ? 0.5796 0.4388 0.6321 0.0377  0.0743  0.0138  203 PHE A C   
1609 O O   . PHE A 202 ? 0.5200 0.3827 0.5795 0.0350  0.0754  0.0015  203 PHE A O   
1610 C CB  . PHE A 202 ? 0.5950 0.4209 0.6541 0.0507  0.0857  0.0306  203 PHE A CB  
1611 C CG  . PHE A 202 ? 0.6122 0.4272 0.6681 0.0618  0.0871  0.0467  203 PHE A CG  
1612 C CD1 . PHE A 202 ? 0.6664 0.4880 0.7094 0.0654  0.0814  0.0592  203 PHE A CD1 
1613 C CD2 . PHE A 202 ? 0.6987 0.4969 0.7644 0.0692  0.0940  0.0493  203 PHE A CD2 
1614 C CE1 . PHE A 202 ? 0.7223 0.5352 0.7611 0.0763  0.0820  0.0744  203 PHE A CE1 
1615 C CE2 . PHE A 202 ? 0.7195 0.5081 0.7821 0.0805  0.0949  0.0652  203 PHE A CE2 
1616 C CZ  . PHE A 202 ? 0.7511 0.5478 0.7998 0.0841  0.0885  0.0780  203 PHE A CZ  
1617 N N   . GLY A 203 ? 0.5784 0.4422 0.6242 0.0315  0.0724  0.0158  204 GLY A N   
1618 C CA  . GLY A 203 ? 0.6146 0.4842 0.6637 0.0206  0.0731  0.0040  204 GLY A CA  
1619 C C   . GLY A 203 ? 0.6756 0.5275 0.7338 0.0147  0.0830  0.0007  204 GLY A C   
1620 O O   . GLY A 203 ? 0.6762 0.5123 0.7344 0.0175  0.0890  0.0109  204 GLY A O   
1621 N N   . TYR A 204 ? 0.6574 0.5124 0.7238 0.0064  0.0849  -0.0138 205 TYR A N   
1622 C CA  . TYR A 204 ? 0.6100 0.4491 0.6877 -0.0005 0.0944  -0.0199 205 TYR A CA  
1623 C C   . TYR A 204 ? 0.7037 0.5530 0.7838 -0.0117 0.0933  -0.0283 205 TYR A C   
1624 O O   . TYR A 204 ? 0.6382 0.5057 0.7162 -0.0152 0.0864  -0.0377 205 TYR A O   
1625 C CB  . TYR A 204 ? 0.6386 0.4704 0.7267 -0.0002 0.0988  -0.0317 205 TYR A CB  
1626 C CG  . TYR A 204 ? 0.6321 0.4502 0.7210 0.0110  0.1021  -0.0226 205 TYR A CG  
1627 C CD1 . TYR A 204 ? 0.5752 0.4048 0.6582 0.0196  0.0954  -0.0195 205 TYR A CD1 
1628 C CD2 . TYR A 204 ? 0.6063 0.4006 0.7026 0.0132  0.1120  -0.0160 205 TYR A CD2 
1629 C CE1 . TYR A 204 ? 0.5576 0.3768 0.6425 0.0305  0.0978  -0.0110 205 TYR A CE1 
1630 C CE2 . TYR A 204 ? 0.6155 0.3979 0.7127 0.0246  0.1145  -0.0067 205 TYR A CE2 
1631 C CZ  . TYR A 204 ? 0.5659 0.3618 0.6577 0.0334  0.1070  -0.0044 205 TYR A CZ  
1632 O OH  . TYR A 204 ? 0.5532 0.3395 0.6472 0.0453  0.1090  0.0049  205 TYR A OH  
1633 N N   . ASN A 205 ? 0.7262 0.5641 0.8107 -0.0168 0.1003  -0.0243 206 ASN A N   
1634 C CA  . ASN A 205 ? 0.7694 0.6172 0.8578 -0.0271 0.0998  -0.0310 206 ASN A CA  
1635 C C   . ASN A 205 ? 0.7907 0.6376 0.8932 -0.0361 0.1035  -0.0482 206 ASN A C   
1636 O O   . ASN A 205 ? 0.7700 0.6092 0.8780 -0.0344 0.1061  -0.0555 206 ASN A O   
1637 C CB  . ASN A 205 ? 0.7595 0.5970 0.8472 -0.0289 0.1063  -0.0196 206 ASN A CB  
1638 C CG  . ASN A 205 ? 0.7893 0.6014 0.8865 -0.0295 0.1185  -0.0157 206 ASN A CG  
1639 O OD1 . ASN A 205 ? 0.8149 0.6174 0.9235 -0.0321 0.1232  -0.0255 206 ASN A OD1 
1640 N ND2 . ASN A 205 ? 0.7753 0.5760 0.8676 -0.0270 0.1242  -0.0011 206 ASN A ND2 
1641 N N   . GLN A 206 ? 0.7878 0.6433 0.8971 -0.0461 0.1038  -0.0556 207 GLN A N   
1642 C CA  . GLN A 206 ? 0.8488 0.7066 0.9717 -0.0555 0.1059  -0.0733 207 GLN A CA  
1643 C C   . GLN A 206 ? 0.8626 0.6960 0.9991 -0.0589 0.1180  -0.0760 207 GLN A C   
1644 O O   . GLN A 206 ? 0.8500 0.6821 0.9977 -0.0652 0.1203  -0.0918 207 GLN A O   
1645 C CB  . GLN A 206 ? 0.8807 0.7555 1.0085 -0.0649 0.1027  -0.0800 207 GLN A CB  
1646 C CG  . GLN A 206 ? 0.8346 0.7332 0.9505 -0.0617 0.0910  -0.0787 207 GLN A CG  
1647 C CD  . GLN A 206 ? 0.8528 0.7590 0.9598 -0.0551 0.0841  -0.0825 207 GLN A CD  
1648 O OE1 . GLN A 206 ? 0.8166 0.7239 0.9117 -0.0464 0.0802  -0.0718 207 GLN A OE1 
1649 N NE2 . GLN A 206 ? 0.8515 0.7636 0.9646 -0.0596 0.0830  -0.0982 207 GLN A NE2 
1650 N N   . GLU A 207 ? 0.9049 0.7189 1.0404 -0.0546 0.1258  -0.0612 208 GLU A N   
1651 C CA  . GLU A 207 ? 0.9053 0.6930 1.0526 -0.0556 0.1379  -0.0608 208 GLU A CA  
1652 C C   . GLU A 207 ? 0.8632 0.6381 1.0056 -0.0440 0.1388  -0.0549 208 GLU A C   
1653 O O   . GLU A 207 ? 0.9357 0.6867 1.0861 -0.0419 0.1489  -0.0507 208 GLU A O   
1654 C CB  . GLU A 207 ? 0.9487 0.7212 1.0985 -0.0576 0.1473  -0.0472 208 GLU A CB  
1655 C CG  . GLU A 207 ? 1.0215 0.7977 1.1853 -0.0714 0.1522  -0.0562 208 GLU A CG  
1656 C CD  . GLU A 207 ? 1.0628 0.8662 1.2209 -0.0752 0.1425  -0.0594 208 GLU A CD  
1657 O OE1 . GLU A 207 ? 1.0220 0.8352 1.1640 -0.0672 0.1355  -0.0480 208 GLU A OE1 
1658 O OE2 . GLU A 207 ? 1.0893 0.9043 1.2597 -0.0860 0.1418  -0.0735 208 GLU A OE2 
1659 N N   . ASN A 208 ? 0.8223 0.6127 0.9527 -0.0362 0.1288  -0.0540 209 ASN A N   
1660 C CA  . ASN A 208 ? 0.8043 0.5873 0.9315 -0.0253 0.1284  -0.0506 209 ASN A CA  
1661 C C   . ASN A 208 ? 0.7675 0.5323 0.8899 -0.0154 0.1334  -0.0310 209 ASN A C   
1662 O O   . ASN A 208 ? 0.7638 0.5123 0.8906 -0.0081 0.1387  -0.0278 209 ASN A O   
1663 C CB  . ASN A 208 ? 0.8312 0.6037 0.9717 -0.0284 0.1343  -0.0664 209 ASN A CB  
1664 C CG  . ASN A 208 ? 0.8191 0.6100 0.9635 -0.0385 0.1293  -0.0863 209 ASN A CG  
1665 O OD1 . ASN A 208 ? 0.7101 0.5213 0.8454 -0.0361 0.1199  -0.0912 209 ASN A OD1 
1666 N ND2 . ASN A 208 ? 0.8038 0.5882 0.9619 -0.0498 0.1355  -0.0978 209 ASN A ND2 
1667 N N   . GLN A 209 ? 0.7842 0.5528 0.8970 -0.0145 0.1316  -0.0176 210 GLN A N   
1668 C CA  . GLN A 209 ? 0.7831 0.5385 0.8880 -0.0044 0.1345  0.0018  210 GLN A CA  
1669 C C   . GLN A 209 ? 0.7472 0.5200 0.8362 0.0047  0.1232  0.0105  210 GLN A C   
1670 O O   . GLN A 209 ? 0.7273 0.5206 0.8097 0.0008  0.1149  0.0059  210 GLN A O   
1671 C CB  . GLN A 209 ? 0.8375 0.5828 0.9420 -0.0093 0.1419  0.0117  210 GLN A CB  
1672 C CG  . GLN A 209 ? 0.8521 0.5840 0.9737 -0.0213 0.1527  0.0016  210 GLN A CG  
1673 C CD  . GLN A 209 ? 0.8966 0.6047 1.0312 -0.0191 0.1623  -0.0012 210 GLN A CD  
1674 O OE1 . GLN A 209 ? 0.9112 0.6072 1.0416 -0.0075 0.1637  0.0100  210 GLN A OE1 
1675 N NE2 . GLN A 209 ? 0.9048 0.6065 1.0560 -0.0302 0.1687  -0.0168 210 GLN A NE2 
1676 N N   . PRO A 210 ? 0.7573 0.5071 0.8368 -0.0213 0.1343  0.0904  211 PRO A N   
1677 C CA  . PRO A 210 ? 0.7505 0.5172 0.8076 -0.0089 0.1289  0.0904  211 PRO A CA  
1678 C C   . PRO A 210 ? 0.7748 0.5538 0.8301 -0.0055 0.1375  0.1016  211 PRO A C   
1679 O O   . PRO A 210 ? 0.8238 0.5902 0.8805 -0.0040 0.1515  0.1145  211 PRO A O   
1680 C CB  . PRO A 210 ? 0.7462 0.4947 0.7791 0.0052  0.1307  0.0938  211 PRO A CB  
1681 C CG  . PRO A 210 ? 0.7667 0.4883 0.8060 0.0029  0.1437  0.1035  211 PRO A CG  
1682 C CD  . PRO A 210 ? 0.7503 0.4707 0.8197 -0.0152 0.1426  0.0971  211 PRO A CD  
1683 N N   . ILE A 211 ? 0.7587 0.5613 0.8101 -0.0039 0.1297  0.0968  212 ILE A N   
1684 C CA  . ILE A 211 ? 0.7860 0.6019 0.8362 -0.0012 0.1364  0.1052  212 ILE A CA  
1685 C C   . ILE A 211 ? 0.8369 0.6670 0.8647 0.0101  0.1286  0.1024  212 ILE A C   
1686 O O   . ILE A 211 ? 0.7691 0.6118 0.7960 0.0085  0.1159  0.0911  212 ILE A O   
1687 C CB  . ILE A 211 ? 0.8076 0.6400 0.8854 -0.0147 0.1356  0.1020  212 ILE A CB  
1688 C CG1 . ILE A 211 ? 0.7658 0.5853 0.8670 -0.0245 0.1477  0.1095  212 ILE A CG1 
1689 C CG2 . ILE A 211 ? 0.8320 0.6834 0.9045 -0.0100 0.1373  0.1060  212 ILE A CG2 
1690 C CD1 . ILE A 211 ? 0.8314 0.6688 0.9610 -0.0359 0.1498  0.1097  212 ILE A CD1 
1691 N N   . ARG A 212 ? 0.8294 0.6569 0.8391 0.0215  0.1362  0.1127  213 ARG A N   
1692 C CA  . ARG A 212 ? 0.8672 0.7075 0.8565 0.0320  0.1293  0.1106  213 ARG A CA  
1693 C C   . ARG A 212 ? 0.8734 0.7179 0.8565 0.0368  0.1389  0.1204  213 ARG A C   
1694 O O   . ARG A 212 ? 0.8759 0.7059 0.8549 0.0409  0.1524  0.1324  213 ARG A O   
1695 C CB  . ARG A 212 ? 0.8640 0.6936 0.8298 0.0452  0.1258  0.1114  213 ARG A CB  
1696 C CG  . ARG A 212 ? 0.8758 0.7194 0.8230 0.0551  0.1167  0.1077  213 ARG A CG  
1697 C CD  . ARG A 212 ? 0.8385 0.6765 0.7709 0.0650  0.1095  0.1044  213 ARG A CD  
1698 N NE  . ARG A 212 ? 0.8148 0.6559 0.7597 0.0575  0.1015  0.0939  213 ARG A NE  
1699 C CZ  . ARG A 212 ? 0.7160 0.5493 0.6542 0.0635  0.0974  0.0908  213 ARG A CZ  
1700 N NH1 . ARG A 212 ? 0.8212 0.6435 0.7417 0.0769  0.0999  0.0975  213 ARG A NH1 
1701 N NH2 . ARG A 212 ? 0.6111 0.4479 0.5601 0.0568  0.0907  0.0807  213 ARG A NH2 
1702 N N   . VAL A 213 ? 0.8936 0.7568 0.8754 0.0369  0.1328  0.1157  214 VAL A N   
1703 C CA  . VAL A 213 ? 0.9193 0.7873 0.8939 0.0423  0.1411  0.1235  214 VAL A CA  
1704 C C   . VAL A 213 ? 0.9129 0.7938 0.8698 0.0500  0.1307  0.1174  214 VAL A C   
1705 O O   . VAL A 213 ? 0.8316 0.7242 0.7929 0.0458  0.1179  0.1065  214 VAL A O   
1706 C CB  . VAL A 213 ? 0.8953 0.7735 0.8963 0.0307  0.1475  0.1252  214 VAL A CB  
1707 C CG1 . VAL A 213 ? 0.8704 0.7684 0.8850 0.0224  0.1347  0.1131  214 VAL A CG1 
1708 C CG2 . VAL A 213 ? 0.8675 0.7462 0.8606 0.0379  0.1604  0.1360  214 VAL A CG2 
1709 N N   . ASN A 214 ? 0.9421 0.8197 0.8784 0.0616  0.1363  0.1244  215 ASN A N   
1710 C CA  . ASN A 214 ? 0.9771 0.8664 0.8986 0.0679  0.1275  0.1187  215 ASN A CA  
1711 C C   . ASN A 214 ? 0.9009 0.8053 0.8385 0.0601  0.1282  0.1160  215 ASN A C   
1712 O O   . ASN A 214 ? 0.8060 0.7109 0.7620 0.0531  0.1385  0.1215  215 ASN A O   
1713 C CB  . ASN A 214 ? 1.0194 0.8985 0.9116 0.0837  0.1326  0.1264  215 ASN A CB  
1714 C CG  . ASN A 214 ? 1.0692 0.9435 0.9411 0.0937  0.1220  0.1225  215 ASN A CG  
1715 O OD1 . ASN A 214 ? 1.0723 0.9570 0.9493 0.0901  0.1088  0.1121  215 ASN A OD1 
1716 N ND2 . ASN A 214 ? 1.1180 0.9772 0.9671 0.1068  0.1282  0.1313  215 ASN A ND2 
1717 N N   . PRO A 215 ? 0.9020 0.8191 0.8347 0.0609  0.1175  0.1075  216 PRO A N   
1718 C CA  . PRO A 215 ? 0.8337 0.7648 0.7817 0.0539  0.1173  0.1045  216 PRO A CA  
1719 C C   . PRO A 215 ? 0.8161 0.7452 0.7582 0.0600  0.1301  0.1135  216 PRO A C   
1720 O O   . PRO A 215 ? 0.8357 0.7536 0.7551 0.0718  0.1364  0.1202  216 PRO A O   
1721 C CB  . PRO A 215 ? 0.7465 0.6877 0.6860 0.0553  0.1032  0.0942  216 PRO A CB  
1722 C CG  . PRO A 215 ? 0.9086 0.8410 0.8236 0.0665  0.0989  0.0942  216 PRO A CG  
1723 C CD  . PRO A 215 ? 0.9329 0.8523 0.8478 0.0677  0.1047  0.1002  216 PRO A CD  
1724 N N   . GLY A 216 ? 0.6790 0.6193 0.6417 0.0526  0.1341  0.1137  217 GLY A N   
1725 C CA  . GLY A 216 ? 0.5703 0.5122 0.5290 0.0585  0.1451  0.1206  217 GLY A CA  
1726 C C   . GLY A 216 ? 0.5143 0.4602 0.4527 0.0667  0.1376  0.1148  217 GLY A C   
1727 O O   . GLY A 216 ? 0.5117 0.4596 0.4409 0.0671  0.1238  0.1057  217 GLY A O   
1728 N N   . PRO A 217 ? 0.4945 0.4414 0.4266 0.0735  0.1471  0.1199  218 PRO A N   
1729 C CA  . PRO A 217 ? 0.4507 0.3992 0.3625 0.0817  0.1402  0.1139  218 PRO A CA  
1730 C C   . PRO A 217 ? 0.4243 0.3867 0.3515 0.0729  0.1277  0.1036  218 PRO A C   
1731 O O   . PRO A 217 ? 0.4416 0.4152 0.3950 0.0633  0.1294  0.1037  218 PRO A O   
1732 C CB  . PRO A 217 ? 0.4577 0.4041 0.3632 0.0902  0.1555  0.1227  218 PRO A CB  
1733 C CG  . PRO A 217 ? 0.4976 0.4495 0.4323 0.0816  0.1682  0.1311  218 PRO A CG  
1734 C CD  . PRO A 217 ? 0.4804 0.4276 0.4257 0.0734  0.1646  0.1311  218 PRO A CD  
1735 N N   . LEU A 218 ? 0.4184 0.3802 0.3296 0.0761  0.1148  0.0948  219 LEU A N   
1736 C CA  . LEU A 218 ? 0.3928 0.3653 0.3150 0.0683  0.1023  0.0851  219 LEU A CA  
1737 C C   . LEU A 218 ? 0.3458 0.3255 0.2911 0.0561  0.0975  0.0825  219 LEU A C   
1738 O O   . LEU A 218 ? 0.3434 0.3336 0.3036 0.0486  0.0911  0.0771  219 LEU A O   
1739 C CB  . LEU A 218 ? 0.4001 0.3804 0.3291 0.0685  0.1050  0.0844  219 LEU A CB  
1740 C CG  . LEU A 218 ? 0.4196 0.3957 0.3274 0.0768  0.0995  0.0789  219 LEU A CG  
1741 C CD1 . LEU A 218 ? 0.5273 0.4897 0.4072 0.0897  0.1046  0.0826  219 LEU A CD1 
1742 C CD2 . LEU A 218 ? 0.3565 0.3394 0.2727 0.0775  0.1040  0.0794  219 LEU A CD2 
1743 N N   . GLY A 219 ? 0.3827 0.3556 0.3292 0.0548  0.1003  0.0860  220 GLY A N   
1744 C CA  . GLY A 219 ? 0.3744 0.3519 0.3409 0.0441  0.0960  0.0831  220 GLY A CA  
1745 C C   . GLY A 219 ? 0.3503 0.3299 0.3128 0.0415  0.0827  0.0742  220 GLY A C   
1746 O O   . GLY A 219 ? 0.3307 0.3175 0.3087 0.0327  0.0769  0.0692  220 GLY A O   
1747 N N   . ALA A 220 ? 0.3479 0.3218 0.2899 0.0494  0.0777  0.0720  221 ALA A N   
1748 C CA  . ALA A 220 ? 0.3023 0.2791 0.2428 0.0472  0.0663  0.0645  221 ALA A CA  
1749 C C   . ALA A 220 ? 0.3216 0.3098 0.2727 0.0401  0.0582  0.0572  221 ALA A C   
1750 O O   . ALA A 220 ? 0.3068 0.2992 0.2677 0.0338  0.0528  0.0528  221 ALA A O   
1751 C CB  . ALA A 220 ? 0.3160 0.2866 0.2346 0.0573  0.0617  0.0633  221 ALA A CB  
1752 N N   . PRO A 221 ? 0.2638 0.2562 0.2128 0.0412  0.0575  0.0558  222 PRO A N   
1753 C CA  . PRO A 221 ? 0.2490 0.2508 0.2079 0.0347  0.0505  0.0498  222 PRO A CA  
1754 C C   . PRO A 221 ? 0.2821 0.2908 0.2608 0.0261  0.0520  0.0502  222 PRO A C   
1755 O O   . PRO A 221 ? 0.2504 0.2659 0.2362 0.0208  0.0455  0.0453  222 PRO A O   
1756 C CB  . PRO A 221 ? 0.2836 0.2856 0.2350 0.0391  0.0514  0.0496  222 PRO A CB  
1757 C CG  . PRO A 221 ? 0.2890 0.2813 0.2219 0.0490  0.0560  0.0532  222 PRO A CG  
1758 C CD  . PRO A 221 ? 0.2825 0.2701 0.2185 0.0493  0.0632  0.0595  222 PRO A CD  
1759 N N   . ALA A 222 ? 0.2650 0.2719 0.2528 0.0247  0.0600  0.0558  223 ALA A N   
1760 C CA  . ALA A 222 ? 0.2602 0.2744 0.2685 0.0164  0.0602  0.0553  223 ALA A CA  
1761 C C   . ALA A 222 ? 0.2850 0.2959 0.3002 0.0110  0.0580  0.0533  223 ALA A C   
1762 O O   . ALA A 222 ? 0.2575 0.2743 0.2842 0.0044  0.0525  0.0487  223 ALA A O   
1763 C CB  . ALA A 222 ? 0.2597 0.2759 0.2790 0.0166  0.0703  0.0622  223 ALA A CB  
1764 N N   . TYR A 223 ? 0.2565 0.2571 0.2633 0.0148  0.0618  0.0564  224 TYR A N   
1765 C CA  . TYR A 223 ? 0.2852 0.2802 0.2978 0.0106  0.0607  0.0548  224 TYR A CA  
1766 C C   . TYR A 223 ? 0.3104 0.2947 0.3078 0.0173  0.0615  0.0564  224 TYR A C   
1767 O O   . TYR A 223 ? 0.3294 0.3053 0.3303 0.0157  0.0640  0.0576  224 TYR A O   
1768 C CB  . TYR A 223 ? 0.2963 0.2888 0.3259 0.0051  0.0683  0.0595  224 TYR A CB  
1769 C CG  . TYR A 223 ? 0.3092 0.2968 0.3357 0.0104  0.0798  0.0688  224 TYR A CG  
1770 C CD1 . TYR A 223 ? 0.4037 0.3780 0.4170 0.0169  0.0861  0.0746  224 TYR A CD1 
1771 C CD2 . TYR A 223 ? 0.3429 0.3388 0.3782 0.0100  0.0848  0.0724  224 TYR A CD2 
1772 C CE1 . TYR A 223 ? 0.4766 0.4452 0.4842 0.0229  0.0977  0.0839  224 TYR A CE1 
1773 C CE2 . TYR A 223 ? 0.4118 0.4028 0.4428 0.0159  0.0969  0.0814  224 TYR A CE2 
1774 C CZ  . TYR A 223 ? 0.4432 0.4202 0.4596 0.0223  0.1034  0.0872  224 TYR A CZ  
1775 O OH  . TYR A 223 ? 0.5762 0.5471 0.5856 0.0293  0.1161  0.0969  224 TYR A OH  
1776 N N   . GLY A 224 ? 0.3298 0.3137 0.3109 0.0248  0.0587  0.0559  225 GLY A N   
1777 C CA  . GLY A 224 ? 0.3258 0.2998 0.2923 0.0328  0.0601  0.0588  225 GLY A CA  
1778 C C   . GLY A 224 ? 0.3303 0.3051 0.2917 0.0346  0.0520  0.0532  225 GLY A C   
1779 O O   . GLY A 224 ? 0.3463 0.3145 0.2950 0.0426  0.0519  0.0553  225 GLY A O   
1780 N N   . VAL A 225 ? 0.2674 0.2502 0.2380 0.0283  0.0457  0.0465  226 VAL A N   
1781 C CA  . VAL A 225 ? 0.2713 0.2566 0.2382 0.0304  0.0390  0.0416  226 VAL A CA  
1782 C C   . VAL A 225 ? 0.2782 0.2568 0.2504 0.0284  0.0404  0.0406  226 VAL A C   
1783 O O   . VAL A 225 ? 0.2527 0.2289 0.2352 0.0218  0.0429  0.0403  226 VAL A O   
1784 C CB  . VAL A 225 ? 0.2403 0.2375 0.2117 0.0261  0.0323  0.0354  226 VAL A CB  
1785 C CG1 . VAL A 225 ? 0.2456 0.2467 0.2162 0.0278  0.0270  0.0309  226 VAL A CG1 
1786 C CG2 . VAL A 225 ? 0.2675 0.2688 0.2327 0.0286  0.0307  0.0359  226 VAL A CG2 
1787 N N   . LYS A 226 ? 0.2832 0.2588 0.2487 0.0344  0.0381  0.0397  227 LYS A N   
1788 C CA  . LYS A 226 ? 0.3099 0.2788 0.2783 0.0342  0.0386  0.0378  227 LYS A CA  
1789 C C   . LYS A 226 ? 0.3033 0.2812 0.2713 0.0363  0.0323  0.0320  227 LYS A C   
1790 O O   . LYS A 226 ? 0.3607 0.3462 0.3239 0.0410  0.0283  0.0316  227 LYS A O   
1791 C CB  . LYS A 226 ? 0.3298 0.2845 0.2903 0.0415  0.0438  0.0438  227 LYS A CB  
1792 C CG  . LYS A 226 ? 0.3379 0.2826 0.2981 0.0408  0.0522  0.0514  227 LYS A CG  
1793 C CD  . LYS A 226 ? 0.4024 0.3497 0.3515 0.0469  0.0533  0.0560  227 LYS A CD  
1794 C CE  . LYS A 226 ? 0.4134 0.3493 0.3600 0.0485  0.0637  0.0650  227 LYS A CE  
1795 N NZ  . LYS A 226 ? 0.4582 0.3991 0.3975 0.0515  0.0653  0.0679  227 LYS A NZ  
1796 N N   . SER A 227 ? 0.2981 0.2751 0.2713 0.0332  0.0314  0.0274  228 SER A N   
1797 C CA  . SER A 227 ? 0.3037 0.2902 0.2775 0.0353  0.0270  0.0226  228 SER A CA  
1798 C C   . SER A 227 ? 0.2958 0.2752 0.2707 0.0359  0.0282  0.0191  228 SER A C   
1799 O O   . SER A 227 ? 0.2954 0.2628 0.2716 0.0328  0.0312  0.0191  228 SER A O   
1800 C CB  . SER A 227 ? 0.2426 0.2416 0.2211 0.0293  0.0237  0.0192  228 SER A CB  
1801 O OG  . SER A 227 ? 0.3056 0.3140 0.2857 0.0313  0.0209  0.0157  228 SER A OG  
1802 N N   . THR A 228 ? 0.3087 0.2953 0.2835 0.0401  0.0261  0.0158  229 THR A N   
1803 C CA  . THR A 228 ? 0.2875 0.2689 0.2619 0.0420  0.0273  0.0116  229 THR A CA  
1804 C C   . THR A 228 ? 0.2980 0.2863 0.2750 0.0361  0.0257  0.0063  229 THR A C   
1805 O O   . THR A 228 ? 0.2855 0.2845 0.2654 0.0317  0.0236  0.0063  229 THR A O   
1806 C CB  . THR A 228 ? 0.2864 0.2727 0.2596 0.0514  0.0268  0.0116  229 THR A CB  
1807 O OG1 . THR A 228 ? 0.2841 0.2880 0.2624 0.0509  0.0239  0.0102  229 THR A OG1 
1808 C CG2 . THR A 228 ? 0.3091 0.2898 0.2778 0.0589  0.0272  0.0172  229 THR A CG2 
1809 N N   . LEU A 229 ? 0.2642 0.2450 0.2387 0.0369  0.0268  0.0016  230 LEU A N   
1810 C CA  . LEU A 229 ? 0.2724 0.2589 0.2461 0.0334  0.0255  -0.0035 230 LEU A CA  
1811 C C   . LEU A 229 ? 0.2605 0.2626 0.2360 0.0366  0.0257  -0.0033 230 LEU A C   
1812 O O   . LEU A 229 ? 0.2800 0.2907 0.2567 0.0320  0.0245  -0.0039 230 LEU A O   
1813 C CB  . LEU A 229 ? 0.2902 0.2638 0.2583 0.0348  0.0263  -0.0094 230 LEU A CB  
1814 C CG  . LEU A 229 ? 0.3034 0.2811 0.2670 0.0324  0.0247  -0.0149 230 LEU A CG  
1815 C CD1 . LEU A 229 ? 0.3054 0.2860 0.2717 0.0239  0.0208  -0.0153 230 LEU A CD1 
1816 C CD2 . LEU A 229 ? 0.3005 0.2645 0.2556 0.0358  0.0252  -0.0219 230 LEU A CD2 
1817 N N   . PRO A 230 ? 0.2691 0.2758 0.2462 0.0441  0.0274  -0.0021 231 PRO A N   
1818 C CA  . PRO A 230 ? 0.2864 0.3100 0.2692 0.0456  0.0278  -0.0016 231 PRO A CA  
1819 C C   . PRO A 230 ? 0.2571 0.2910 0.2456 0.0403  0.0247  0.0015  231 PRO A C   
1820 O O   . PRO A 230 ? 0.2943 0.3384 0.2864 0.0369  0.0250  0.0012  231 PRO A O   
1821 C CB  . PRO A 230 ? 0.3188 0.3458 0.3050 0.0548  0.0290  -0.0004 231 PRO A CB  
1822 C CG  . PRO A 230 ? 0.2984 0.3078 0.2768 0.0591  0.0310  -0.0022 231 PRO A CG  
1823 C CD  . PRO A 230 ? 0.2985 0.2956 0.2731 0.0519  0.0293  -0.0016 231 PRO A CD  
1824 N N   . ASP A 231 ? 0.2496 0.2798 0.2379 0.0399  0.0222  0.0045  232 ASP A N   
1825 C CA  . ASP A 231 ? 0.2508 0.2886 0.2424 0.0355  0.0192  0.0067  232 ASP A CA  
1826 C C   . ASP A 231 ? 0.2574 0.2941 0.2477 0.0279  0.0192  0.0059  232 ASP A C   
1827 O O   . ASP A 231 ? 0.2294 0.2747 0.2232 0.0242  0.0179  0.0064  232 ASP A O   
1828 C CB  . ASP A 231 ? 0.2396 0.2713 0.2279 0.0379  0.0174  0.0100  232 ASP A CB  
1829 C CG  . ASP A 231 ? 0.3005 0.3388 0.2910 0.0450  0.0147  0.0113  232 ASP A CG  
1830 O OD1 . ASP A 231 ? 0.3434 0.3902 0.3397 0.0486  0.0149  0.0095  232 ASP A OD1 
1831 O OD2 . ASP A 231 ? 0.3402 0.3752 0.3262 0.0477  0.0124  0.0140  232 ASP A OD2 
1832 N N   . MET A 232 ? 0.2465 0.2725 0.2326 0.0255  0.0201  0.0046  233 MET A N   
1833 C CA  . MET A 232 ? 0.2424 0.2685 0.2280 0.0189  0.0190  0.0038  233 MET A CA  
1834 C C   . MET A 232 ? 0.2572 0.2894 0.2413 0.0180  0.0196  0.0012  233 MET A C   
1835 O O   . MET A 232 ? 0.2650 0.3021 0.2496 0.0140  0.0185  0.0018  233 MET A O   
1836 C CB  . MET A 232 ? 0.2675 0.2822 0.2516 0.0161  0.0189  0.0025  233 MET A CB  
1837 C CG  . MET A 232 ? 0.2536 0.2625 0.2397 0.0155  0.0197  0.0068  233 MET A CG  
1838 S SD  . MET A 232 ? 0.2704 0.2881 0.2587 0.0133  0.0184  0.0107  233 MET A SD  
1839 C CE  . MET A 232 ? 0.2638 0.2841 0.2552 0.0064  0.0166  0.0088  233 MET A CE  
1840 N N   . LEU A 233 ? 0.2624 0.2941 0.2440 0.0226  0.0220  -0.0014 234 LEU A N   
1841 C CA  . LEU A 233 ? 0.2853 0.3231 0.2644 0.0230  0.0242  -0.0028 234 LEU A CA  
1842 C C   . LEU A 233 ? 0.2606 0.3114 0.2473 0.0220  0.0253  0.0006  234 LEU A C   
1843 O O   . LEU A 233 ? 0.2524 0.3078 0.2381 0.0194  0.0267  0.0015  234 LEU A O   
1844 C CB  . LEU A 233 ? 0.2610 0.2953 0.2354 0.0292  0.0277  -0.0060 234 LEU A CB  
1845 C CG  . LEU A 233 ? 0.2702 0.2901 0.2358 0.0295  0.0262  -0.0109 234 LEU A CG  
1846 C CD1 . LEU A 233 ? 0.3146 0.3293 0.2742 0.0369  0.0299  -0.0145 234 LEU A CD1 
1847 C CD2 . LEU A 233 ? 0.2934 0.3113 0.2527 0.0248  0.0233  -0.0133 234 LEU A CD2 
1848 N N   . SER A 234 ? 0.2341 0.2904 0.2284 0.0243  0.0245  0.0025  235 SER A N   
1849 C CA  . SER A 234 ? 0.2407 0.3087 0.2442 0.0221  0.0240  0.0049  235 SER A CA  
1850 C C   . SER A 234 ? 0.2367 0.3035 0.2393 0.0160  0.0213  0.0065  235 SER A C   
1851 O O   . SER A 234 ? 0.2242 0.2970 0.2308 0.0126  0.0222  0.0079  235 SER A O   
1852 C CB  . SER A 234 ? 0.2650 0.3386 0.2762 0.0259  0.0214  0.0056  235 SER A CB  
1853 O OG  . SER A 234 ? 0.3732 0.4515 0.3882 0.0320  0.0243  0.0048  235 SER A OG  
1854 N N   . PHE A 235 ? 0.2280 0.2866 0.2260 0.0149  0.0185  0.0066  236 PHE A N   
1855 C CA  . PHE A 235 ? 0.2545 0.3119 0.2517 0.0103  0.0164  0.0081  236 PHE A CA  
1856 C C   . PHE A 235 ? 0.2506 0.3075 0.2440 0.0071  0.0177  0.0079  236 PHE A C   
1857 O O   . PHE A 235 ? 0.1980 0.2577 0.1927 0.0040  0.0173  0.0098  236 PHE A O   
1858 C CB  . PHE A 235 ? 0.2172 0.2664 0.2111 0.0104  0.0147  0.0088  236 PHE A CB  
1859 C CG  . PHE A 235 ? 0.2082 0.2564 0.2016 0.0067  0.0133  0.0106  236 PHE A CG  
1860 C CD1 . PHE A 235 ? 0.2319 0.2840 0.2275 0.0059  0.0116  0.0118  236 PHE A CD1 
1861 C CD2 . PHE A 235 ? 0.2477 0.2910 0.2393 0.0044  0.0132  0.0107  236 PHE A CD2 
1862 C CE1 . PHE A 235 ? 0.2426 0.2927 0.2367 0.0036  0.0108  0.0132  236 PHE A CE1 
1863 C CE2 . PHE A 235 ? 0.2356 0.2792 0.2279 0.0020  0.0123  0.0126  236 PHE A CE2 
1864 C CZ  . PHE A 235 ? 0.2557 0.3020 0.2483 0.0021  0.0115  0.0140  236 PHE A CZ  
1865 N N   . ILE A 236 ? 0.2206 0.2732 0.2083 0.0085  0.0189  0.0056  237 ILE A N   
1866 C CA  . ILE A 236 ? 0.2523 0.3042 0.2338 0.0070  0.0193  0.0051  237 ILE A CA  
1867 C C   . ILE A 236 ? 0.2558 0.3146 0.2383 0.0076  0.0235  0.0071  237 ILE A C   
1868 O O   . ILE A 236 ? 0.2582 0.3180 0.2379 0.0056  0.0242  0.0093  237 ILE A O   
1869 C CB  . ILE A 236 ? 0.2407 0.2854 0.2145 0.0088  0.0185  0.0009  237 ILE A CB  
1870 C CG1 . ILE A 236 ? 0.2972 0.3350 0.2729 0.0067  0.0149  -0.0006 237 ILE A CG1 
1871 C CG2 . ILE A 236 ? 0.2423 0.2865 0.2070 0.0089  0.0183  -0.0001 237 ILE A CG2 
1872 C CD1 . ILE A 236 ? 0.3366 0.3753 0.3151 0.0025  0.0117  0.0012  237 ILE A CD1 
1873 N N   . HIS A 237 ? 0.2143 0.2780 0.2015 0.0107  0.0269  0.0069  238 HIS A N   
1874 C CA  . HIS A 237 ? 0.2515 0.3235 0.2438 0.0108  0.0320  0.0096  238 HIS A CA  
1875 C C   . HIS A 237 ? 0.2099 0.2862 0.2104 0.0058  0.0307  0.0128  238 HIS A C   
1876 O O   . HIS A 237 ? 0.2261 0.3046 0.2269 0.0038  0.0344  0.0159  238 HIS A O   
1877 C CB  . HIS A 237 ? 0.2571 0.3358 0.2572 0.0150  0.0351  0.0089  238 HIS A CB  
1878 C CG  . HIS A 237 ? 0.2917 0.3813 0.3020 0.0143  0.0407  0.0121  238 HIS A CG  
1879 N ND1 . HIS A 237 ? 0.3310 0.4214 0.3357 0.0157  0.0477  0.0142  238 HIS A ND1 
1880 C CD2 . HIS A 237 ? 0.2674 0.3675 0.2938 0.0123  0.0405  0.0137  238 HIS A CD2 
1881 C CE1 . HIS A 237 ? 0.3793 0.4804 0.3976 0.0142  0.0528  0.0177  238 HIS A CE1 
1882 N NE2 . HIS A 237 ? 0.3037 0.4114 0.3364 0.0117  0.0480  0.0170  238 HIS A NE2 
1883 N N   . ALA A 238 ? 0.2027 0.2791 0.2089 0.0044  0.0259  0.0122  239 ALA A N   
1884 C CA  . ALA A 238 ? 0.2279 0.3064 0.2405 0.0000  0.0239  0.0141  239 ALA A CA  
1885 C C   . ALA A 238 ? 0.2249 0.2971 0.2299 -0.0027 0.0235  0.0159  239 ALA A C   
1886 O O   . ALA A 238 ? 0.2005 0.2734 0.2088 -0.0059 0.0247  0.0184  239 ALA A O   
1887 C CB  . ALA A 238 ? 0.2055 0.2834 0.2216 0.0005  0.0183  0.0125  239 ALA A CB  
1888 N N   . ASN A 239 ? 0.2011 0.2671 0.1970 -0.0013 0.0217  0.0147  240 ASN A N   
1889 C CA  . ASN A 239 ? 0.2292 0.2908 0.2187 -0.0029 0.0207  0.0164  240 ASN A CA  
1890 C C   . ASN A 239 ? 0.2386 0.3002 0.2215 -0.0019 0.0248  0.0184  240 ASN A C   
1891 O O   . ASN A 239 ? 0.2240 0.2832 0.2033 -0.0031 0.0252  0.0214  240 ASN A O   
1892 C CB  . ASN A 239 ? 0.2173 0.2742 0.2021 -0.0020 0.0169  0.0142  240 ASN A CB  
1893 C CG  . ASN A 239 ? 0.2371 0.2923 0.2260 -0.0031 0.0141  0.0146  240 ASN A CG  
1894 O OD1 . ASN A 239 ? 0.2640 0.3176 0.2523 -0.0043 0.0129  0.0164  240 ASN A OD1 
1895 N ND2 . ASN A 239 ? 0.2195 0.2744 0.2113 -0.0017 0.0135  0.0132  240 ASN A ND2 
1896 N N   . LEU A 240 ? 0.2394 0.3029 0.2193 0.0011  0.0283  0.0171  241 LEU A N   
1897 C CA  . LEU A 240 ? 0.2677 0.3308 0.2393 0.0033  0.0335  0.0194  241 LEU A CA  
1898 C C   . LEU A 240 ? 0.2919 0.3601 0.2718 0.0011  0.0399  0.0242  241 LEU A C   
1899 O O   . LEU A 240 ? 0.2675 0.3335 0.2410 0.0016  0.0444  0.0284  241 LEU A O   
1900 C CB  . LEU A 240 ? 0.2749 0.3374 0.2394 0.0082  0.0359  0.0160  241 LEU A CB  
1901 C CG  . LEU A 240 ? 0.3004 0.3558 0.2538 0.0104  0.0304  0.0110  241 LEU A CG  
1902 C CD1 . LEU A 240 ? 0.2526 0.3061 0.2019 0.0149  0.0322  0.0066  241 LEU A CD1 
1903 C CD2 . LEU A 240 ? 0.2661 0.3172 0.2056 0.0122  0.0293  0.0120  241 LEU A CD2 
1904 N N   . ASN A 241 ? 0.2672 0.3419 0.2616 -0.0012 0.0402  0.0239  242 ASN A N   
1905 C CA  . ASN A 241 ? 0.2721 0.3531 0.2785 -0.0042 0.0459  0.0279  242 ASN A CA  
1906 C C   . ASN A 241 ? 0.2652 0.3491 0.2857 -0.0091 0.0411  0.0269  242 ASN A C   
1907 O O   . ASN A 241 ? 0.2487 0.3413 0.2833 -0.0101 0.0413  0.0257  242 ASN A O   
1908 C CB  . ASN A 241 ? 0.2791 0.3682 0.2909 -0.0009 0.0525  0.0281  242 ASN A CB  
1909 C CG  . ASN A 241 ? 0.4106 0.4957 0.4068 0.0043  0.0588  0.0297  242 ASN A CG  
1910 O OD1 . ASN A 241 ? 0.4513 0.5349 0.4437 0.0039  0.0653  0.0350  242 ASN A OD1 
1911 N ND2 . ASN A 241 ? 0.4266 0.5085 0.4122 0.0095  0.0568  0.0252  242 ASN A ND2 
1912 N N   . PRO A 242 ? 0.2316 0.3085 0.2485 -0.0116 0.0365  0.0269  243 PRO A N   
1913 C CA  . PRO A 242 ? 0.2551 0.3330 0.2825 -0.0153 0.0312  0.0250  243 PRO A CA  
1914 C C   . PRO A 242 ? 0.2625 0.3458 0.3053 -0.0203 0.0344  0.0269  243 PRO A C   
1915 O O   . PRO A 242 ? 0.2463 0.3340 0.3009 -0.0227 0.0295  0.0238  243 PRO A O   
1916 C CB  . PRO A 242 ? 0.2408 0.3089 0.2589 -0.0159 0.0275  0.0254  243 PRO A CB  
1917 C CG  . PRO A 242 ? 0.2609 0.3245 0.2674 -0.0139 0.0315  0.0289  243 PRO A CG  
1918 C CD  . PRO A 242 ? 0.2477 0.3158 0.2505 -0.0103 0.0351  0.0283  243 PRO A CD  
1919 N N   . GLN A 243 ? 0.2327 0.3157 0.2759 -0.0217 0.0423  0.0321  244 GLN A N   
1920 C CA  . GLN A 243 ? 0.2697 0.3575 0.3300 -0.0275 0.0467  0.0349  244 GLN A CA  
1921 C C   . GLN A 243 ? 0.2581 0.3603 0.3363 -0.0278 0.0474  0.0328  244 GLN A C   
1922 O O   . GLN A 243 ? 0.2883 0.3969 0.3855 -0.0335 0.0485  0.0334  244 GLN A O   
1923 C CB  . GLN A 243 ? 0.2690 0.3525 0.3243 -0.0279 0.0570  0.0423  244 GLN A CB  
1924 C CG  . GLN A 243 ? 0.2911 0.3806 0.3417 -0.0227 0.0657  0.0452  244 GLN A CG  
1925 C CD  . GLN A 243 ? 0.2988 0.3834 0.3281 -0.0154 0.0632  0.0428  244 GLN A CD  
1926 O OE1 . GLN A 243 ? 0.2699 0.3476 0.2892 -0.0144 0.0554  0.0395  244 GLN A OE1 
1927 N NE2 . GLN A 243 ? 0.3415 0.4296 0.3644 -0.0102 0.0701  0.0442  244 GLN A NE2 
1928 N N   . LYS A 244 ? 0.2616 0.3691 0.3352 -0.0219 0.0464  0.0301  245 LYS A N   
1929 C CA  . LYS A 244 ? 0.2321 0.3537 0.3224 -0.0208 0.0467  0.0281  245 LYS A CA  
1930 C C   . LYS A 244 ? 0.2699 0.3952 0.3682 -0.0213 0.0358  0.0223  245 LYS A C   
1931 O O   . LYS A 244 ? 0.2727 0.4107 0.3868 -0.0203 0.0342  0.0203  245 LYS A O   
1932 C CB  . LYS A 244 ? 0.2608 0.3851 0.3418 -0.0132 0.0514  0.0281  245 LYS A CB  
1933 C CG  . LYS A 244 ? 0.3396 0.4633 0.4150 -0.0116 0.0632  0.0338  245 LYS A CG  
1934 C CD  . LYS A 244 ? 0.4352 0.5582 0.4970 -0.0033 0.0671  0.0327  245 LYS A CD  
1935 C CE  . LYS A 244 ? 0.4988 0.6220 0.5552 -0.0009 0.0796  0.0385  245 LYS A CE  
1936 N NZ  . LYS A 244 ? 0.6120 0.7466 0.6917 -0.0062 0.0868  0.0434  245 LYS A NZ  
1937 N N   . TYR A 245 ? 0.2311 0.3459 0.3187 -0.0219 0.0284  0.0196  246 TYR A N   
1938 C CA  . TYR A 245 ? 0.2280 0.3432 0.3172 -0.0208 0.0182  0.0143  246 TYR A CA  
1939 C C   . TYR A 245 ? 0.2233 0.3367 0.3225 -0.0273 0.0129  0.0122  246 TYR A C   
1940 O O   . TYR A 245 ? 0.2256 0.3326 0.3254 -0.0324 0.0168  0.0152  246 TYR A O   
1941 C CB  . TYR A 245 ? 0.2113 0.3152 0.2805 -0.0162 0.0147  0.0130  246 TYR A CB  
1942 C CG  . TYR A 245 ? 0.2062 0.3114 0.2677 -0.0099 0.0175  0.0132  246 TYR A CG  
1943 C CD1 . TYR A 245 ? 0.2320 0.3362 0.2876 -0.0087 0.0252  0.0162  246 TYR A CD1 
1944 C CD2 . TYR A 245 ? 0.2070 0.3132 0.2660 -0.0047 0.0124  0.0103  246 TYR A CD2 
1945 C CE1 . TYR A 245 ? 0.2343 0.3383 0.2826 -0.0029 0.0272  0.0153  246 TYR A CE1 
1946 C CE2 . TYR A 245 ? 0.2242 0.3298 0.2767 0.0008  0.0152  0.0103  246 TYR A CE2 
1947 C CZ  . TYR A 245 ? 0.2216 0.3258 0.2690 0.0015  0.0223  0.0124  246 TYR A CZ  
1948 O OH  . TYR A 245 ? 0.2552 0.3572 0.2957 0.0071  0.0244  0.0114  246 TYR A OH  
1949 N N   . PRO A 246 ? 0.2209 0.3387 0.3273 -0.0268 0.0036  0.0069  247 PRO A N   
1950 C CA  . PRO A 246 ? 0.2324 0.3473 0.3476 -0.0328 -0.0030 0.0034  247 PRO A CA  
1951 C C   . PRO A 246 ? 0.2064 0.3043 0.3044 -0.0334 -0.0042 0.0035  247 PRO A C   
1952 O O   . PRO A 246 ? 0.2259 0.3160 0.3058 -0.0283 -0.0028 0.0049  247 PRO A O   
1953 C CB  . PRO A 246 ? 0.2325 0.3544 0.3523 -0.0291 -0.0141 -0.0030 247 PRO A CB  
1954 C CG  . PRO A 246 ? 0.2231 0.3565 0.3460 -0.0230 -0.0110 -0.0014 247 PRO A CG  
1955 C CD  . PRO A 246 ? 0.2149 0.3406 0.3220 -0.0202 -0.0016 0.0038  247 PRO A CD  
1956 N N   . ALA A 247 ? 0.2117 0.3040 0.3170 -0.0398 -0.0068 0.0017  248 ALA A N   
1957 C CA  . ALA A 247 ? 0.2262 0.3024 0.3182 -0.0411 -0.0052 0.0033  248 ALA A CA  
1958 C C   . ALA A 247 ? 0.2443 0.3109 0.3158 -0.0344 -0.0101 0.0007  248 ALA A C   
1959 O O   . ALA A 247 ? 0.2334 0.2912 0.2910 -0.0319 -0.0057 0.0043  248 ALA A O   
1960 C CB  . ALA A 247 ? 0.2446 0.3152 0.3487 -0.0489 -0.0085 0.0006  248 ALA A CB  
1961 N N   . ASP A 248 ? 0.2269 0.2954 0.2963 -0.0308 -0.0190 -0.0052 249 ASP A N   
1962 C CA  . ASP A 248 ? 0.2630 0.3211 0.3126 -0.0242 -0.0223 -0.0069 249 ASP A CA  
1963 C C   . ASP A 248 ? 0.2627 0.3209 0.3006 -0.0188 -0.0161 -0.0020 249 ASP A C   
1964 O O   . ASP A 248 ? 0.2466 0.2954 0.2712 -0.0160 -0.0138 -0.0001 249 ASP A O   
1965 C CB  . ASP A 248 ? 0.2922 0.3518 0.3395 -0.0201 -0.0326 -0.0136 249 ASP A CB  
1966 C CG  . ASP A 248 ? 0.3345 0.3894 0.3890 -0.0249 -0.0407 -0.0203 249 ASP A CG  
1967 O OD1 . ASP A 248 ? 0.3144 0.3603 0.3712 -0.0305 -0.0381 -0.0195 249 ASP A OD1 
1968 O OD2 . ASP A 248 ? 0.3818 0.4412 0.4394 -0.0229 -0.0505 -0.0266 249 ASP A OD2 
1969 N N   . ILE A 249 ? 0.2531 0.3218 0.2968 -0.0173 -0.0135 -0.0003 250 ILE A N   
1970 C CA  . ILE A 249 ? 0.2192 0.2866 0.2526 -0.0130 -0.0084 0.0034  250 ILE A CA  
1971 C C   . ILE A 249 ? 0.2230 0.2891 0.2564 -0.0161 -0.0008 0.0082  250 ILE A C   
1972 O O   . ILE A 249 ? 0.2002 0.2612 0.2232 -0.0137 0.0022  0.0107  250 ILE A O   
1973 C CB  . ILE A 249 ? 0.2355 0.3117 0.2717 -0.0086 -0.0089 0.0029  250 ILE A CB  
1974 C CG1 . ILE A 249 ? 0.2478 0.3194 0.2720 -0.0039 -0.0052 0.0055  250 ILE A CG1 
1975 C CG2 . ILE A 249 ? 0.2140 0.3018 0.2654 -0.0116 -0.0052 0.0041  250 ILE A CG2 
1976 C CD1 . ILE A 249 ? 0.2180 0.2799 0.2289 0.0000  -0.0073 0.0053  250 ILE A CD1 
1977 N N   . GLN A 250 ? 0.2180 0.2885 0.2630 -0.0213 0.0024  0.0098  251 GLN A N   
1978 C CA  A GLN A 250 ? 0.2295 0.2969 0.2717 -0.0233 0.0097  0.0148  251 GLN A CA  
1979 C CA  B GLN A 250 ? 0.2262 0.2936 0.2686 -0.0234 0.0097  0.0148  251 GLN A CA  
1980 C C   . GLN A 250 ? 0.2207 0.2762 0.2520 -0.0232 0.0093  0.0161  251 GLN A C   
1981 O O   . GLN A 250 ? 0.2273 0.2794 0.2491 -0.0208 0.0126  0.0193  251 GLN A O   
1982 C CB  A GLN A 250 ? 0.2068 0.2795 0.2635 -0.0290 0.0141  0.0171  251 GLN A CB  
1983 C CB  B GLN A 250 ? 0.2030 0.2754 0.2600 -0.0292 0.0138  0.0169  251 GLN A CB  
1984 C CG  A GLN A 250 ? 0.2443 0.3116 0.2955 -0.0302 0.0221  0.0232  251 GLN A CG  
1985 C CG  B GLN A 250 ? 0.2446 0.3101 0.2972 -0.0314 0.0209  0.0227  251 GLN A CG  
1986 C CD  A GLN A 250 ? 0.2515 0.3240 0.3166 -0.0352 0.0290  0.0271  251 GLN A CD  
1987 C CD  B GLN A 250 ? 0.2448 0.3078 0.3101 -0.0383 0.0227  0.0241  251 GLN A CD  
1988 O OE1 A GLN A 250 ? 0.2401 0.3069 0.3005 -0.0361 0.0360  0.0328  251 GLN A OE1 
1989 O OE1 B GLN A 250 ? 0.2329 0.2889 0.3001 -0.0409 0.0171  0.0207  251 GLN A OE1 
1990 N NE2 A GLN A 250 ? 0.2340 0.3175 0.3167 -0.0380 0.0275  0.0246  251 GLN A NE2 
1991 N NE2 B GLN A 250 ? 0.2707 0.3385 0.3447 -0.0411 0.0310  0.0291  251 GLN A NE2 
1992 N N   . ARG A 251 ? 0.2132 0.2623 0.2458 -0.0251 0.0048  0.0133  252 ARG A N   
1993 C CA  . ARG A 251 ? 0.2271 0.2646 0.2496 -0.0239 0.0047  0.0144  252 ARG A CA  
1994 C C   . ARG A 251 ? 0.2168 0.2521 0.2272 -0.0179 0.0035  0.0141  252 ARG A C   
1995 O O   . ARG A 251 ? 0.2462 0.2766 0.2491 -0.0158 0.0060  0.0172  252 ARG A O   
1996 C CB  . ARG A 251 ? 0.2561 0.2859 0.2816 -0.0266 -0.0003 0.0102  252 ARG A CB  
1997 C CG  . ARG A 251 ? 0.3098 0.3391 0.3487 -0.0339 0.0022  0.0116  252 ARG A CG  
1998 C CD  . ARG A 251 ? 0.3042 0.3307 0.3524 -0.0381 -0.0048 0.0052  252 ARG A CD  
1999 N NE  . ARG A 251 ? 0.3537 0.3670 0.3900 -0.0351 -0.0101 0.0010  252 ARG A NE  
2000 C CZ  . ARG A 251 ? 0.3808 0.3803 0.4142 -0.0371 -0.0091 0.0014  252 ARG A CZ  
2001 N NH1 . ARG A 251 ? 0.3621 0.3581 0.4022 -0.0420 -0.0025 0.0070  252 ARG A NH1 
2002 N NH2 . ARG A 251 ? 0.3571 0.3449 0.3796 -0.0335 -0.0144 -0.0036 252 ARG A NH2 
2003 N N   . ALA A 252 ? 0.2199 0.2593 0.2292 -0.0148 0.0000  0.0109  253 ALA A N   
2004 C CA  . ALA A 252 ? 0.2149 0.2525 0.2146 -0.0095 0.0002  0.0116  253 ALA A CA  
2005 C C   . ALA A 252 ? 0.2493 0.2904 0.2478 -0.0091 0.0047  0.0152  253 ALA A C   
2006 O O   . ALA A 252 ? 0.2213 0.2592 0.2140 -0.0069 0.0060  0.0172  253 ALA A O   
2007 C CB  . ALA A 252 ? 0.1963 0.2374 0.1952 -0.0061 -0.0034 0.0086  253 ALA A CB  
2008 N N   . ILE A 253 ? 0.2160 0.2640 0.2200 -0.0108 0.0067  0.0158  254 ILE A N   
2009 C CA  . ILE A 253 ? 0.2108 0.2611 0.2117 -0.0097 0.0099  0.0179  254 ILE A CA  
2010 C C   . ILE A 253 ? 0.2429 0.2894 0.2397 -0.0105 0.0121  0.0212  254 ILE A C   
2011 O O   . ILE A 253 ? 0.2328 0.2784 0.2246 -0.0085 0.0121  0.0222  254 ILE A O   
2012 C CB  . ILE A 253 ? 0.2504 0.3079 0.2567 -0.0103 0.0121  0.0176  254 ILE A CB  
2013 C CG1 . ILE A 253 ? 0.2265 0.2877 0.2354 -0.0077 0.0096  0.0147  254 ILE A CG1 
2014 C CG2 . ILE A 253 ? 0.2321 0.2900 0.2328 -0.0091 0.0153  0.0192  254 ILE A CG2 
2015 C CD1 . ILE A 253 ? 0.2421 0.3116 0.2594 -0.0081 0.0115  0.0142  254 ILE A CD1 
2016 N N   . ASN A 254 ? 0.2353 0.2796 0.2350 -0.0134 0.0138  0.0229  255 ASN A N   
2017 C CA  . ASN A 254 ? 0.2539 0.2932 0.2483 -0.0132 0.0162  0.0268  255 ASN A CA  
2018 C C   . ASN A 254 ? 0.2589 0.2926 0.2481 -0.0105 0.0138  0.0270  255 ASN A C   
2019 O O   . ASN A 254 ? 0.2449 0.2774 0.2288 -0.0081 0.0142  0.0296  255 ASN A O   
2020 C CB  . ASN A 254 ? 0.2361 0.2722 0.2355 -0.0171 0.0192  0.0292  255 ASN A CB  
2021 C CG  . ASN A 254 ? 0.2960 0.3380 0.2992 -0.0187 0.0242  0.0313  255 ASN A CG  
2022 O OD1 . ASN A 254 ? 0.3155 0.3598 0.3117 -0.0158 0.0263  0.0329  255 ASN A OD1 
2023 N ND2 . ASN A 254 ? 0.2649 0.3098 0.2796 -0.0230 0.0260  0.0312  255 ASN A ND2 
2024 N N   . GLU A 255 ? 0.2383 0.2690 0.2285 -0.0100 0.0111  0.0242  256 GLU A N   
2025 C CA  . GLU A 255 ? 0.2489 0.2749 0.2343 -0.0063 0.0100  0.0245  256 GLU A CA  
2026 C C   . GLU A 255 ? 0.2458 0.2770 0.2299 -0.0036 0.0100  0.0253  256 GLU A C   
2027 O O   . GLU A 255 ? 0.2368 0.2668 0.2191 -0.0008 0.0101  0.0272  256 GLU A O   
2028 C CB  . GLU A 255 ? 0.2513 0.2731 0.2357 -0.0052 0.0074  0.0209  256 GLU A CB  
2029 C CG  . GLU A 255 ? 0.2789 0.2929 0.2575 -0.0013 0.0074  0.0212  256 GLU A CG  
2030 C CD  . GLU A 255 ? 0.3009 0.3062 0.2784 -0.0025 0.0081  0.0226  256 GLU A CD  
2031 O OE1 . GLU A 255 ? 0.3364 0.3378 0.3173 -0.0067 0.0070  0.0209  256 GLU A OE1 
2032 O OE2 . GLU A 255 ? 0.3474 0.3498 0.3215 0.0009  0.0098  0.0257  256 GLU A OE2 
2033 N N   . THR A 256 ? 0.2450 0.2819 0.2313 -0.0043 0.0098  0.0237  257 THR A N   
2034 C CA  . THR A 256 ? 0.2204 0.2610 0.2073 -0.0027 0.0096  0.0240  257 THR A CA  
2035 C C   . THR A 256 ? 0.2434 0.2866 0.2288 -0.0029 0.0092  0.0254  257 THR A C   
2036 O O   . THR A 256 ? 0.2809 0.3275 0.2681 -0.0022 0.0078  0.0249  257 THR A O   
2037 C CB  . THR A 256 ? 0.2192 0.2626 0.2080 -0.0029 0.0095  0.0218  257 THR A CB  
2038 O OG1 . THR A 256 ? 0.2070 0.2534 0.1963 -0.0046 0.0099  0.0207  257 THR A OG1 
2039 C CG2 . THR A 256 ? 0.2215 0.2621 0.2095 -0.0016 0.0090  0.0204  257 THR A CG2 
2040 N N   . HIS A 257 ? 0.2036 0.2452 0.1859 -0.0037 0.0104  0.0271  258 HIS A N   
2041 C CA  . HIS A 257 ? 0.2309 0.2741 0.2086 -0.0026 0.0099  0.0285  258 HIS A CA  
2042 C C   . HIS A 257 ? 0.2690 0.3094 0.2432 0.0001  0.0091  0.0319  258 HIS A C   
2043 O O   . HIS A 257 ? 0.2807 0.3228 0.2499 0.0023  0.0073  0.0329  258 HIS A O   
2044 C CB  . HIS A 257 ? 0.2447 0.2876 0.2193 -0.0040 0.0132  0.0294  258 HIS A CB  
2045 C CG  . HIS A 257 ? 0.2387 0.2856 0.2162 -0.0051 0.0139  0.0262  258 HIS A CG  
2046 N ND1 . HIS A 257 ? 0.2400 0.2885 0.2171 -0.0059 0.0177  0.0268  258 HIS A ND1 
2047 C CD2 . HIS A 257 ? 0.2150 0.2642 0.1962 -0.0052 0.0120  0.0229  258 HIS A CD2 
2048 C CE1 . HIS A 257 ? 0.2470 0.2990 0.2272 -0.0058 0.0175  0.0235  258 HIS A CE1 
2049 N NE2 . HIS A 257 ? 0.2344 0.2860 0.2165 -0.0055 0.0140  0.0213  258 HIS A NE2 
2050 N N   . GLN A 258 ? 0.2768 0.3125 0.2523 0.0008  0.0098  0.0334  259 GLN A N   
2051 C CA  . GLN A 258 ? 0.2815 0.3133 0.2534 0.0042  0.0096  0.0369  259 GLN A CA  
2052 C C   . GLN A 258 ? 0.2440 0.2816 0.2194 0.0076  0.0063  0.0367  259 GLN A C   
2053 O O   . GLN A 258 ? 0.2339 0.2737 0.2152 0.0076  0.0064  0.0350  259 GLN A O   
2054 C CB  . GLN A 258 ? 0.3076 0.3306 0.2795 0.0039  0.0117  0.0379  259 GLN A CB  
2055 C CG  . GLN A 258 ? 0.3899 0.4064 0.3572 0.0079  0.0122  0.0420  259 GLN A CG  
2056 C CD  . GLN A 258 ? 0.4660 0.4722 0.4330 0.0083  0.0137  0.0417  259 GLN A CD  
2057 O OE1 . GLN A 258 ? 0.4911 0.4934 0.4603 0.0042  0.0144  0.0388  259 GLN A OE1 
2058 N NE2 . GLN A 258 ? 0.4626 0.4643 0.4270 0.0136  0.0137  0.0441  259 GLN A NE2 
2059 N N   . GLY A 259 ? 0.2942 0.3347 0.2664 0.0107  0.0035  0.0385  260 GLY A N   
2060 C CA  . GLY A 259 ? 0.2853 0.3329 0.2639 0.0139  -0.0001 0.0385  260 GLY A CA  
2061 C C   . GLY A 259 ? 0.2737 0.3181 0.2552 0.0174  0.0019  0.0409  260 GLY A C   
2062 O O   . GLY A 259 ? 0.2646 0.3004 0.2396 0.0197  0.0040  0.0439  260 GLY A O   
2063 N N   . ARG A 260 ? 0.2344 0.2851 0.2256 0.0182  0.0020  0.0399  261 ARG A N   
2064 C CA  . ARG A 260 ? 0.2225 0.2705 0.2161 0.0226  0.0049  0.0420  261 ARG A CA  
2065 C C   . ARG A 260 ? 0.2651 0.3212 0.2657 0.0282  0.0024  0.0446  261 ARG A C   
2066 O O   . ARG A 260 ? 0.2691 0.3207 0.2678 0.0337  0.0044  0.0473  261 ARG A O   
2067 C CB  . ARG A 260 ? 0.2041 0.2527 0.2027 0.0212  0.0086  0.0401  261 ARG A CB  
2068 C CG  . ARG A 260 ? 0.2438 0.2852 0.2360 0.0167  0.0101  0.0374  261 ARG A CG  
2069 C CD  . ARG A 260 ? 0.2770 0.3066 0.2600 0.0169  0.0112  0.0376  261 ARG A CD  
2070 N NE  . ARG A 260 ? 0.2874 0.3133 0.2677 0.0122  0.0114  0.0346  261 ARG A NE  
2071 C CZ  . ARG A 260 ? 0.3006 0.3172 0.2762 0.0111  0.0120  0.0332  261 ARG A CZ  
2072 N NH1 . ARG A 260 ? 0.3007 0.3082 0.2722 0.0143  0.0130  0.0342  261 ARG A NH1 
2073 N NH2 . ARG A 260 ? 0.2889 0.3053 0.2648 0.0068  0.0114  0.0304  261 ARG A NH2 
2074 N N   . TYR A 261 ? 0.2092 0.2770 0.2182 0.0271  -0.0024 0.0433  262 TYR A N   
2075 C CA  . TYR A 261 ? 0.2123 0.2905 0.2300 0.0320  -0.0068 0.0451  262 TYR A CA  
2076 C C   . TYR A 261 ? 0.2106 0.2983 0.2332 0.0287  -0.0140 0.0416  262 TYR A C   
2077 O O   . TYR A 261 ? 0.2073 0.2924 0.2261 0.0231  -0.0143 0.0383  262 TYR A O   
2078 C CB  . TYR A 261 ? 0.2087 0.2945 0.2410 0.0348  -0.0031 0.0466  262 TYR A CB  
2079 C CG  . TYR A 261 ? 0.1999 0.2914 0.2434 0.0291  -0.0002 0.0443  262 TYR A CG  
2080 C CD1 . TYR A 261 ? 0.1957 0.2989 0.2526 0.0249  -0.0051 0.0417  262 TYR A CD1 
2081 C CD2 . TYR A 261 ? 0.1980 0.2819 0.2380 0.0284  0.0072  0.0446  262 TYR A CD2 
2082 C CE1 . TYR A 261 ? 0.1896 0.2961 0.2569 0.0196  -0.0017 0.0403  262 TYR A CE1 
2083 C CE2 . TYR A 261 ? 0.1924 0.2800 0.2411 0.0242  0.0105  0.0435  262 TYR A CE2 
2084 C CZ  . TYR A 261 ? 0.1881 0.2866 0.2508 0.0195  0.0066  0.0418  262 TYR A CZ  
2085 O OH  . TYR A 261 ? 0.1844 0.2848 0.2560 0.0152  0.0107  0.0414  262 TYR A OH  
2086 N N   . GLN A 262 ? 0.2141 0.3130 0.2456 0.0325  -0.0203 0.0420  263 GLN A N   
2087 C CA  . GLN A 262 ? 0.2163 0.3237 0.2511 0.0305  -0.0292 0.0379  263 GLN A CA  
2088 C C   . GLN A 262 ? 0.2117 0.3353 0.2700 0.0293  -0.0329 0.0363  263 GLN A C   
2089 O O   . GLN A 262 ? 0.2112 0.3421 0.2809 0.0340  -0.0311 0.0399  263 GLN A O   
2090 C CB  . GLN A 262 ? 0.2535 0.3589 0.2743 0.0370  -0.0357 0.0395  263 GLN A CB  
2091 C CG  . GLN A 262 ? 0.2925 0.4047 0.3120 0.0363  -0.0461 0.0345  263 GLN A CG  
2092 C CD  . GLN A 262 ? 0.3518 0.4586 0.3515 0.0437  -0.0510 0.0368  263 GLN A CD  
2093 O OE1 . GLN A 262 ? 0.3472 0.4463 0.3374 0.0495  -0.0468 0.0429  263 GLN A OE1 
2094 N NE2 . GLN A 262 ? 0.4246 0.5337 0.4167 0.0439  -0.0595 0.0320  263 GLN A NE2 
2095 N N   . VAL A 263 ? 0.2092 0.3385 0.2759 0.0229  -0.0377 0.0310  264 VAL A N   
2096 C CA  . VAL A 263 ? 0.2072 0.3527 0.2982 0.0206  -0.0432 0.0285  264 VAL A CA  
2097 C C   . VAL A 263 ? 0.2420 0.3908 0.3295 0.0189  -0.0554 0.0220  264 VAL A C   
2098 O O   . VAL A 263 ? 0.2395 0.3823 0.3224 0.0129  -0.0563 0.0171  264 VAL A O   
2099 C CB  . VAL A 263 ? 0.2870 0.4347 0.3946 0.0135  -0.0361 0.0281  264 VAL A CB  
2100 C CG1 . VAL A 263 ? 0.2772 0.4421 0.4127 0.0100  -0.0418 0.0258  264 VAL A CG1 
2101 C CG2 . VAL A 263 ? 0.2633 0.4068 0.3711 0.0166  -0.0244 0.0342  264 VAL A CG2 
2102 N N   . ASN A 264 ? 0.2875 0.4450 0.3755 0.0251  -0.0651 0.0217  265 ASN A N   
2103 C CA  . ASN A 264 ? 0.2809 0.4413 0.3626 0.0255  -0.0783 0.0151  265 ASN A CA  
2104 C C   . ASN A 264 ? 0.2774 0.4209 0.3304 0.0258  -0.0763 0.0138  265 ASN A C   
2105 O O   . ASN A 264 ? 0.3162 0.4497 0.3507 0.0314  -0.0706 0.0194  265 ASN A O   
2106 C CB  . ASN A 264 ? 0.2939 0.4656 0.3998 0.0172  -0.0847 0.0082  265 ASN A CB  
2107 C CG  . ASN A 264 ? 0.3821 0.5713 0.5191 0.0164  -0.0840 0.0109  265 ASN A CG  
2108 O OD1 . ASN A 264 ? 0.4125 0.6066 0.5710 0.0086  -0.0793 0.0100  265 ASN A OD1 
2109 N ND2 . ASN A 264 ? 0.3612 0.5598 0.5012 0.0251  -0.0877 0.0148  265 ASN A ND2 
2110 N N   . THR A 265 ? 0.2642 0.4034 0.3131 0.0202  -0.0798 0.0069  266 THR A N   
2111 C CA  . THR A 265 ? 0.2920 0.4165 0.3145 0.0214  -0.0775 0.0057  266 THR A CA  
2112 C C   . THR A 265 ? 0.2500 0.3639 0.2690 0.0164  -0.0648 0.0082  266 THR A C   
2113 O O   . THR A 265 ? 0.2840 0.3868 0.2839 0.0169  -0.0615 0.0075  266 THR A O   
2114 C CB  . THR A 265 ? 0.2926 0.4169 0.3100 0.0194  -0.0882 -0.0037 266 THR A CB  
2115 O OG1 . THR A 265 ? 0.3232 0.4539 0.3643 0.0106  -0.0902 -0.0090 266 THR A OG1 
2116 C CG2 . THR A 265 ? 0.3288 0.4605 0.3405 0.0268  -0.1016 -0.0061 266 THR A CG2 
2117 N N   . MET A 266 ? 0.2573 0.3745 0.2937 0.0122  -0.0576 0.0110  267 MET A N   
2118 C CA  A MET A 266 ? 0.2385 0.3463 0.2717 0.0082  -0.0468 0.0131  267 MET A CA  
2119 C CA  B MET A 266 ? 0.2377 0.3454 0.2707 0.0083  -0.0468 0.0131  267 MET A CA  
2120 C C   . MET A 266 ? 0.2472 0.3505 0.2750 0.0122  -0.0385 0.0204  267 MET A C   
2121 O O   . MET A 266 ? 0.2511 0.3608 0.2874 0.0159  -0.0386 0.0241  267 MET A O   
2122 C CB  A MET A 266 ? 0.2313 0.3435 0.2850 0.0014  -0.0441 0.0113  267 MET A CB  
2123 C CB  B MET A 266 ? 0.2316 0.3435 0.2848 0.0014  -0.0439 0.0113  267 MET A CB  
2124 C CG  A MET A 266 ? 0.2683 0.3710 0.3180 -0.0020 -0.0343 0.0128  267 MET A CG  
2125 C CG  B MET A 266 ? 0.2690 0.3706 0.3171 -0.0022 -0.0343 0.0125  267 MET A CG  
2126 S SD  A MET A 266 ? 0.3520 0.4586 0.4243 -0.0090 -0.0309 0.0117  267 MET A SD  
2127 S SD  B MET A 266 ? 0.2520 0.3515 0.3034 -0.0003 -0.0231 0.0198  267 MET A SD  
2128 C CE  A MET A 266 ? 0.2586 0.3773 0.3498 -0.0064 -0.0277 0.0176  267 MET A CE  
2129 C CE  B MET A 266 ? 0.2489 0.3624 0.3258 -0.0009 -0.0238 0.0217  267 MET A CE  
2130 N N   . TYR A 267 ? 0.2128 0.3051 0.2272 0.0114  -0.0316 0.0220  268 TYR A N   
2131 C CA  . TYR A 267 ? 0.2103 0.2963 0.2202 0.0137  -0.0239 0.0275  268 TYR A CA  
2132 C C   . TYR A 267 ? 0.2342 0.3167 0.2495 0.0091  -0.0170 0.0271  268 TYR A C   
2133 O O   . TYR A 267 ? 0.2482 0.3269 0.2598 0.0053  -0.0162 0.0240  268 TYR A O   
2134 C CB  . TYR A 267 ? 0.2577 0.3340 0.2490 0.0165  -0.0217 0.0300  268 TYR A CB  
2135 C CG  . TYR A 267 ? 0.2878 0.3651 0.2690 0.0224  -0.0278 0.0313  268 TYR A CG  
2136 C CD1 . TYR A 267 ? 0.3235 0.4028 0.2977 0.0228  -0.0345 0.0269  268 TYR A CD1 
2137 C CD2 . TYR A 267 ? 0.3316 0.4064 0.3086 0.0283  -0.0269 0.0368  268 TYR A CD2 
2138 C CE1 . TYR A 267 ? 0.3332 0.4128 0.2954 0.0295  -0.0406 0.0281  268 TYR A CE1 
2139 C CE2 . TYR A 267 ? 0.3661 0.4410 0.3320 0.0348  -0.0324 0.0387  268 TYR A CE2 
2140 C CZ  . TYR A 267 ? 0.3844 0.4620 0.3425 0.0356  -0.0394 0.0344  268 TYR A CZ  
2141 O OH  . TYR A 267 ? 0.3902 0.4673 0.3348 0.0434  -0.0454 0.0363  268 TYR A OH  
2142 N N   . GLN A 268 ? 0.1954 0.2790 0.2188 0.0102  -0.0123 0.0302  269 GLN A N   
2143 C CA  . GLN A 268 ? 0.1892 0.2688 0.2155 0.0073  -0.0059 0.0303  269 GLN A CA  
2144 C C   . GLN A 268 ? 0.2161 0.2852 0.2294 0.0082  -0.0015 0.0317  269 GLN A C   
2145 O O   . GLN A 268 ? 0.2184 0.2837 0.2273 0.0120  0.0003  0.0346  269 GLN A O   
2146 C CB  . GLN A 268 ? 0.1864 0.2714 0.2256 0.0089  -0.0020 0.0330  269 GLN A CB  
2147 C CG  . GLN A 268 ? 0.1830 0.2629 0.2227 0.0072  0.0049  0.0336  269 GLN A CG  
2148 C CD  . GLN A 268 ? 0.2199 0.3015 0.2665 0.0019  0.0044  0.0309  269 GLN A CD  
2149 O OE1 . GLN A 268 ? 0.2064 0.2961 0.2675 -0.0005 0.0024  0.0303  269 GLN A OE1 
2150 N NE2 . GLN A 268 ? 0.2050 0.2787 0.2420 -0.0001 0.0058  0.0290  269 GLN A NE2 
2151 N N   . ALA A 269 ? 0.2348 0.2993 0.2430 0.0048  -0.0001 0.0294  270 ALA A N   
2152 C CA  . ALA A 269 ? 0.2351 0.2916 0.2352 0.0047  0.0037  0.0299  270 ALA A CA  
2153 C C   . ALA A 269 ? 0.2365 0.2911 0.2399 0.0043  0.0075  0.0297  270 ALA A C   
2154 O O   . ALA A 269 ? 0.2319 0.2907 0.2436 0.0045  0.0087  0.0303  270 ALA A O   
2155 C CB  . ALA A 269 ? 0.2332 0.2871 0.2262 0.0023  0.0029  0.0280  270 ALA A CB  
2156 N N   . LEU A 270 ? 0.2577 0.3060 0.2548 0.0039  0.0094  0.0289  271 LEU A N   
2157 C CA  . LEU A 270 ? 0.2397 0.2857 0.2370 0.0045  0.0122  0.0284  271 LEU A CA  
2158 C C   . LEU A 270 ? 0.2286 0.2769 0.2290 0.0018  0.0118  0.0266  271 LEU A C   
2159 O O   . LEU A 270 ? 0.2718 0.3191 0.2688 -0.0001 0.0104  0.0245  271 LEU A O   
2160 C CB  . LEU A 270 ? 0.2816 0.3207 0.2713 0.0053  0.0125  0.0272  271 LEU A CB  
2161 C CG  . LEU A 270 ? 0.3166 0.3500 0.3020 0.0082  0.0131  0.0281  271 LEU A CG  
2162 C CD1 . LEU A 270 ? 0.3065 0.3331 0.2859 0.0077  0.0119  0.0253  271 LEU A CD1 
2163 C CD2 . LEU A 270 ? 0.3157 0.3492 0.3023 0.0127  0.0163  0.0301  271 LEU A CD2 
2164 N N   . GLY A 271 ? 0.2047 0.2555 0.2120 0.0017  0.0137  0.0276  272 GLY A N   
2165 C CA  . GLY A 271 ? 0.2203 0.2715 0.2313 -0.0010 0.0136  0.0260  272 GLY A CA  
2166 C C   . GLY A 271 ? 0.2192 0.2744 0.2338 -0.0040 0.0092  0.0234  272 GLY A C   
2167 O O   . GLY A 271 ? 0.2302 0.2886 0.2541 -0.0062 0.0083  0.0228  272 GLY A O   
2168 N N   . TRP A 272 ? 0.2152 0.2699 0.2227 -0.0041 0.0066  0.0216  273 TRP A N   
2169 C CA  . TRP A 272 ? 0.2027 0.2597 0.2093 -0.0055 0.0023  0.0188  273 TRP A CA  
2170 C C   . TRP A 272 ? 0.1930 0.2557 0.2050 -0.0050 -0.0014 0.0194  273 TRP A C   
2171 O O   . TRP A 272 ? 0.2023 0.2665 0.2146 -0.0026 -0.0006 0.0226  273 TRP A O   
2172 C CB  . TRP A 272 ? 0.1850 0.2400 0.1816 -0.0046 0.0021  0.0183  273 TRP A CB  
2173 C CG  . TRP A 272 ? 0.2593 0.3112 0.2525 -0.0049 0.0048  0.0171  273 TRP A CG  
2174 C CD1 . TRP A 272 ? 0.2513 0.3015 0.2427 -0.0043 0.0073  0.0185  273 TRP A CD1 
2175 C CD2 . TRP A 272 ? 0.2276 0.2779 0.2195 -0.0055 0.0046  0.0138  273 TRP A CD2 
2176 N NE1 . TRP A 272 ? 0.2750 0.3246 0.2655 -0.0043 0.0086  0.0167  273 TRP A NE1 
2177 C CE2 . TRP A 272 ? 0.2098 0.2589 0.1999 -0.0046 0.0075  0.0140  273 TRP A CE2 
2178 C CE3 . TRP A 272 ? 0.2033 0.2528 0.1957 -0.0064 0.0019  0.0102  273 TRP A CE3 
2179 C CZ2 . TRP A 272 ? 0.2398 0.2874 0.2285 -0.0038 0.0085  0.0115  273 TRP A CZ2 
2180 C CZ3 . TRP A 272 ? 0.1948 0.2409 0.1845 -0.0059 0.0030  0.0072  273 TRP A CZ3 
2181 C CH2 . TRP A 272 ? 0.2159 0.2612 0.2036 -0.0042 0.0067  0.0083  273 TRP A CH2 
2182 N N   . GLU A 273 ? 0.2085 0.2742 0.2246 -0.0069 -0.0061 0.0159  274 GLU A N   
2183 C CA  . GLU A 273 ? 0.2405 0.3123 0.2593 -0.0059 -0.0121 0.0151  274 GLU A CA  
2184 C C   . GLU A 273 ? 0.2806 0.3496 0.2849 -0.0036 -0.0153 0.0133  274 GLU A C   
2185 O O   . GLU A 273 ? 0.3011 0.3652 0.2977 -0.0043 -0.0143 0.0106  274 GLU A O   
2186 C CB  . GLU A 273 ? 0.2573 0.3338 0.2891 -0.0094 -0.0167 0.0114  274 GLU A CB  
2187 C CG  . GLU A 273 ? 0.3333 0.4126 0.3805 -0.0117 -0.0121 0.0142  274 GLU A CG  
2188 C CD  . GLU A 273 ? 0.3811 0.4657 0.4449 -0.0164 -0.0163 0.0108  274 GLU A CD  
2189 O OE1 . GLU A 273 ? 0.4179 0.5020 0.4799 -0.0182 -0.0237 0.0048  274 GLU A OE1 
2190 O OE2 . GLU A 273 ? 0.3873 0.4764 0.4665 -0.0181 -0.0121 0.0141  274 GLU A OE2 
2191 N N   . GLU A 274 ? 0.2560 0.3278 0.2560 0.0000  -0.0183 0.0154  275 GLU A N   
2192 C CA  . GLU A 274 ? 0.2728 0.3405 0.2569 0.0034  -0.0190 0.0161  275 GLU A CA  
2193 C C   . GLU A 274 ? 0.3049 0.3769 0.2853 0.0067  -0.0274 0.0140  275 GLU A C   
2194 O O   . GLU A 274 ? 0.2389 0.3184 0.2305 0.0072  -0.0321 0.0140  275 GLU A O   
2195 C CB  . GLU A 274 ? 0.3047 0.3684 0.2837 0.0057  -0.0135 0.0220  275 GLU A CB  
2196 C CG  . GLU A 274 ? 0.3482 0.4067 0.3119 0.0091  -0.0120 0.0247  275 GLU A CG  
2197 C CD  . GLU A 274 ? 0.4074 0.4611 0.3692 0.0105  -0.0070 0.0304  275 GLU A CD  
2198 O OE1 . GLU A 274 ? 0.3857 0.4396 0.3564 0.0089  -0.0048 0.0313  275 GLU A OE1 
2199 O OE2 . GLU A 274 ? 0.4874 0.5362 0.4383 0.0134  -0.0051 0.0341  275 GLU A OE2 
2200 N N   . PHE A 275 ? 0.2557 0.3233 0.2204 0.0094  -0.0292 0.0121  276 PHE A N   
2201 C CA  . PHE A 275 ? 0.2746 0.3448 0.2314 0.0137  -0.0381 0.0092  276 PHE A CA  
2202 C C   . PHE A 275 ? 0.2703 0.3337 0.2056 0.0196  -0.0356 0.0125  276 PHE A C   
2203 O O   . PHE A 275 ? 0.3282 0.3854 0.2559 0.0190  -0.0275 0.0148  276 PHE A O   
2204 C CB  . PHE A 275 ? 0.3193 0.3901 0.2779 0.0110  -0.0449 0.0006  276 PHE A CB  
2205 C CG  . PHE A 275 ? 0.3251 0.4008 0.3051 0.0045  -0.0457 -0.0020 276 PHE A CG  
2206 C CD1 . PHE A 275 ? 0.2992 0.3845 0.2950 0.0033  -0.0529 -0.0036 276 PHE A CD1 
2207 C CD2 . PHE A 275 ? 0.3142 0.3852 0.2992 0.0001  -0.0386 -0.0022 276 PHE A CD2 
2208 C CE1 . PHE A 275 ? 0.3558 0.4455 0.3726 -0.0029 -0.0520 -0.0049 276 PHE A CE1 
2209 C CE2 . PHE A 275 ? 0.3525 0.4267 0.3560 -0.0053 -0.0380 -0.0034 276 PHE A CE2 
2210 C CZ  . PHE A 275 ? 0.3142 0.3976 0.3338 -0.0070 -0.0441 -0.0044 276 PHE A CZ  
2211 N N   . SER A 276 ? 0.3218 0.3870 0.2480 0.0256  -0.0423 0.0133  277 SER A N   
2212 C CA  . SER A 276 ? 0.3251 0.3830 0.2281 0.0323  -0.0405 0.0160  277 SER A CA  
2213 C C   . SER A 276 ? 0.3686 0.4225 0.2595 0.0328  -0.0426 0.0091  277 SER A C   
2214 O O   . SER A 276 ? 0.3656 0.4232 0.2611 0.0314  -0.0520 0.0011  277 SER A O   
2215 C CB  . SER A 276 ? 0.3613 0.4217 0.2557 0.0400  -0.0484 0.0182  277 SER A CB  
2216 O OG  . SER A 276 ? 0.3853 0.4373 0.2547 0.0473  -0.0459 0.0214  277 SER A OG  
2217 N N   . TYR A 277 ? 0.3621 0.4083 0.2384 0.0349  -0.0335 0.0121  278 TYR A N   
2218 C CA  . TYR A 277 ? 0.3543 0.3956 0.2168 0.0370  -0.0341 0.0059  278 TYR A CA  
2219 C C   . TYR A 277 ? 0.3948 0.4313 0.2316 0.0467  -0.0381 0.0062  278 TYR A C   
2220 O O   . TYR A 277 ? 0.4128 0.4462 0.2389 0.0518  -0.0332 0.0145  278 TYR A O   
2221 C CB  . TYR A 277 ? 0.4147 0.4516 0.2764 0.0347  -0.0216 0.0086  278 TYR A CB  
2222 C CG  . TYR A 277 ? 0.4156 0.4466 0.2604 0.0388  -0.0203 0.0034  278 TYR A CG  
2223 C CD1 . TYR A 277 ? 0.4335 0.4640 0.2840 0.0357  -0.0247 -0.0056 278 TYR A CD1 
2224 C CD2 . TYR A 277 ? 0.4856 0.5106 0.3080 0.0465  -0.0141 0.0076  278 TYR A CD2 
2225 C CE1 . TYR A 277 ? 0.4453 0.4691 0.2792 0.0403  -0.0236 -0.0111 278 TYR A CE1 
2226 C CE2 . TYR A 277 ? 0.5101 0.5292 0.3154 0.0515  -0.0122 0.0026  278 TYR A CE2 
2227 C CZ  . TYR A 277 ? 0.5355 0.5539 0.3466 0.0485  -0.0173 -0.0071 278 TYR A CZ  
2228 O OH  . TYR A 277 ? 0.5709 0.5821 0.3643 0.0542  -0.0154 -0.0127 278 TYR A OH  
2229 N N   . PRO A 278 ? 0.4429 0.4773 0.2680 0.0500  -0.0470 -0.0028 279 PRO A N   
2230 C CA  . PRO A 278 ? 0.3733 0.4096 0.2102 0.0444  -0.0544 -0.0134 279 PRO A CA  
2231 C C   . PRO A 278 ? 0.3729 0.4188 0.2308 0.0395  -0.0659 -0.0173 279 PRO A C   
2232 O O   . PRO A 278 ? 0.3596 0.4104 0.2153 0.0438  -0.0742 -0.0162 279 PRO A O   
2233 C CB  . PRO A 278 ? 0.4102 0.4385 0.2216 0.0518  -0.0600 -0.0211 279 PRO A CB  
2234 C CG  . PRO A 278 ? 0.4665 0.4919 0.2545 0.0619  -0.0602 -0.0152 279 PRO A CG  
2235 C CD  . PRO A 278 ? 0.4414 0.4681 0.2363 0.0605  -0.0476 -0.0026 279 PRO A CD  
2236 N N   . ALA A 279 ? 0.3753 0.4242 0.2548 0.0309  -0.0660 -0.0213 280 ALA A N   
2237 C CA  . ALA A 279 ? 0.3444 0.4028 0.2465 0.0255  -0.0758 -0.0254 280 ALA A CA  
2238 C C   . ALA A 279 ? 0.3821 0.4384 0.2825 0.0244  -0.0879 -0.0375 280 ALA A C   
2239 O O   . ALA A 279 ? 0.4043 0.4520 0.2994 0.0225  -0.0852 -0.0429 280 ALA A O   
2240 C CB  . ALA A 279 ? 0.3394 0.4013 0.2657 0.0169  -0.0682 -0.0222 280 ALA A CB  
2241 N N   . THR A 280 ? 0.3481 0.4120 0.2535 0.0258  -0.1015 -0.0420 281 THR A N   
2242 C CA  . THR A 280 ? 0.3624 0.4252 0.2708 0.0232  -0.1146 -0.0546 281 THR A CA  
2243 C C   . THR A 280 ? 0.3643 0.4277 0.2991 0.0120  -0.1119 -0.0578 281 THR A C   
2244 O O   . THR A 280 ? 0.3370 0.4051 0.2903 0.0068  -0.1024 -0.0504 281 THR A O   
2245 C CB  . THR A 280 ? 0.4151 0.4890 0.3299 0.0257  -0.1306 -0.0586 281 THR A CB  
2246 O OG1 . THR A 280 ? 0.3872 0.4749 0.3330 0.0194  -0.1295 -0.0535 281 THR A OG1 
2247 C CG2 . THR A 280 ? 0.4351 0.5080 0.3228 0.0380  -0.1328 -0.0538 281 THR A CG2 
2248 N N   . LEU A 281 ? 0.3753 0.4322 0.3103 0.0087  -0.1201 -0.0692 282 LEU A N   
2249 C CA  . LEU A 281 ? 0.4322 0.4881 0.3925 -0.0019 -0.1181 -0.0724 282 LEU A CA  
2250 C C   . LEU A 281 ? 0.3926 0.4641 0.3854 -0.0088 -0.1216 -0.0693 282 LEU A C   
2251 O O   . LEU A 281 ? 0.4253 0.4989 0.4388 -0.0156 -0.1124 -0.0640 282 LEU A O   
2252 C CB  . LEU A 281 ? 0.3914 0.4364 0.3461 -0.0040 -0.1280 -0.0861 282 LEU A CB  
2253 C CG  . LEU A 281 ? 0.3777 0.4182 0.3568 -0.0149 -0.1261 -0.0901 282 LEU A CG  
2254 C CD1 . LEU A 281 ? 0.3826 0.4169 0.3632 -0.0165 -0.1087 -0.0812 282 LEU A CD1 
2255 C CD2 . LEU A 281 ? 0.4798 0.5068 0.4499 -0.0160 -0.1367 -0.1045 282 LEU A CD2 
2256 N N   . GLN A 282 ? 0.3669 0.4497 0.3638 -0.0060 -0.1345 -0.0721 283 GLN A N   
2257 C CA  . GLN A 282 ? 0.4172 0.5170 0.4462 -0.0114 -0.1378 -0.0689 283 GLN A CA  
2258 C C   . GLN A 282 ? 0.4196 0.5255 0.4556 -0.0102 -0.1238 -0.0554 283 GLN A C   
2259 O O   . GLN A 282 ? 0.4157 0.5294 0.4784 -0.0169 -0.1182 -0.0511 283 GLN A O   
2260 C CB  . GLN A 282 ? 0.4194 0.5307 0.4486 -0.0066 -0.1549 -0.0742 283 GLN A CB  
2261 C CG  . GLN A 282 ? 0.5214 0.6514 0.5884 -0.0134 -0.1611 -0.0741 283 GLN A CG  
2262 C CD  . GLN A 282 ? 0.5255 0.6536 0.6193 -0.0260 -0.1607 -0.0800 283 GLN A CD  
2263 O OE1 . GLN A 282 ? 0.4734 0.6058 0.5905 -0.0327 -0.1492 -0.0728 283 GLN A OE1 
2264 N NE2 . GLN A 282 ? 0.5040 0.6242 0.5933 -0.0290 -0.1731 -0.0931 283 GLN A NE2 
2265 N N   . THR A 283 ? 0.3919 0.4936 0.4040 -0.0016 -0.1177 -0.0486 284 THR A N   
2266 C CA  . THR A 283 ? 0.3994 0.5043 0.4164 -0.0006 -0.1048 -0.0369 284 THR A CA  
2267 C C   . THR A 283 ? 0.4235 0.5220 0.4501 -0.0074 -0.0920 -0.0337 284 THR A C   
2268 O O   . THR A 283 ? 0.3651 0.4697 0.4095 -0.0105 -0.0845 -0.0270 284 THR A O   
2269 C CB  . THR A 283 ? 0.3442 0.4427 0.3332 0.0088  -0.1001 -0.0309 284 THR A CB  
2270 O OG1 . THR A 283 ? 0.3969 0.5024 0.3786 0.0161  -0.1113 -0.0318 284 THR A OG1 
2271 C CG2 . THR A 283 ? 0.3722 0.4707 0.3648 0.0090  -0.0865 -0.0201 284 THR A CG2 
2272 N N   . LEU A 284 ? 0.4071 0.4928 0.4213 -0.0089 -0.0893 -0.0384 285 LEU A N   
2273 C CA  . LEU A 284 ? 0.4185 0.4975 0.4399 -0.0141 -0.0777 -0.0352 285 LEU A CA  
2274 C C   . LEU A 284 ? 0.4207 0.5038 0.4698 -0.0229 -0.0791 -0.0377 285 LEU A C   
2275 O O   . LEU A 284 ? 0.3860 0.4697 0.4482 -0.0265 -0.0692 -0.0315 285 LEU A O   
2276 C CB  . LEU A 284 ? 0.3697 0.4345 0.3708 -0.0122 -0.0744 -0.0393 285 LEU A CB  
2277 C CG  . LEU A 284 ? 0.3894 0.4496 0.3648 -0.0041 -0.0697 -0.0354 285 LEU A CG  
2278 C CD1 . LEU A 284 ? 0.3807 0.4284 0.3382 -0.0019 -0.0671 -0.0405 285 LEU A CD1 
2279 C CD2 . LEU A 284 ? 0.3690 0.4318 0.3468 -0.0033 -0.0584 -0.0250 285 LEU A CD2 
2280 N N   . LEU A 285 ? 0.3766 0.4623 0.4347 -0.0263 -0.0914 -0.0468 286 LEU A N   
2281 C CA  . LEU A 285 ? 0.3887 0.4793 0.4764 -0.0356 -0.0932 -0.0492 286 LEU A CA  
2282 C C   . LEU A 285 ? 0.4664 0.5733 0.5778 -0.0370 -0.0905 -0.0416 286 LEU A C   
2283 O O   . LEU A 285 ? 0.4479 0.5574 0.5814 -0.0432 -0.0828 -0.0374 286 LEU A O   
2284 C CB  . LEU A 285 ? 0.3781 0.4684 0.4706 -0.0389 -0.1088 -0.0617 286 LEU A CB  
2285 C CG  . LEU A 285 ? 0.4093 0.4815 0.4830 -0.0390 -0.1112 -0.0707 286 LEU A CG  
2286 C CD1 . LEU A 285 ? 0.3984 0.4701 0.4771 -0.0423 -0.1282 -0.0842 286 LEU A CD1 
2287 C CD2 . LEU A 285 ? 0.4368 0.4975 0.5185 -0.0448 -0.0992 -0.0678 286 LEU A CD2 
2288 N N   . ASP A 286 ? 0.3929 0.5104 0.4994 -0.0305 -0.0960 -0.0394 287 ASP A N   
2289 C CA  . ASP A 286 ? 0.3851 0.5188 0.5140 -0.0305 -0.0942 -0.0327 287 ASP A CA  
2290 C C   . ASP A 286 ? 0.4018 0.5333 0.5315 -0.0295 -0.0781 -0.0220 287 ASP A C   
2291 O O   . ASP A 286 ? 0.3845 0.5260 0.5374 -0.0322 -0.0727 -0.0167 287 ASP A O   
2292 C CB  . ASP A 286 ? 0.4390 0.5825 0.5590 -0.0222 -0.1036 -0.0325 287 ASP A CB  
2293 C CG  . ASP A 286 ? 0.4904 0.6425 0.6195 -0.0235 -0.1213 -0.0426 287 ASP A CG  
2294 O OD1 . ASP A 286 ? 0.4631 0.6146 0.6095 -0.0322 -0.1261 -0.0499 287 ASP A OD1 
2295 O OD2 . ASP A 286 ? 0.5232 0.6821 0.6421 -0.0157 -0.1307 -0.0433 287 ASP A OD2 
2296 N N   . SER A 287 ? 0.3654 0.4841 0.4706 -0.0255 -0.0704 -0.0190 288 SER A N   
2297 C CA  . SER A 287 ? 0.4394 0.5546 0.5434 -0.0244 -0.0566 -0.0102 288 SER A CA  
2298 C C   . SER A 287 ? 0.5140 0.6268 0.6359 -0.0313 -0.0488 -0.0085 288 SER A C   
2299 O O   . SER A 287 ? 0.4588 0.5714 0.5844 -0.0303 -0.0381 -0.0010 288 SER A O   
2300 C CB  . SER A 287 ? 0.4438 0.5462 0.5208 -0.0199 -0.0512 -0.0087 288 SER A CB  
2301 O OG  . SER A 287 ? 0.4191 0.5101 0.4899 -0.0235 -0.0496 -0.0132 288 SER A OG  
2302 N N   . ASN A 288 ? 0.5716 0.6810 0.7032 -0.0378 -0.0538 -0.0152 289 ASN A N   
2303 C CA  . ASN A 288 ? 0.5975 0.7034 0.7474 -0.0449 -0.0465 -0.0134 289 ASN A CA  
2304 C C   . ASN A 288 ? 0.5412 0.6594 0.7221 -0.0519 -0.0524 -0.0161 289 ASN A C   
2305 O O   . ASN A 288 ? 0.5427 0.6563 0.7399 -0.0594 -0.0494 -0.0173 289 ASN A O   
2306 C CB  . ASN A 288 ? 0.6287 0.7178 0.7659 -0.0473 -0.0455 -0.0183 289 ASN A CB  
2307 C CG  . ASN A 288 ? 0.7452 0.8238 0.8616 -0.0422 -0.0353 -0.0129 289 ASN A CG  
2308 O OD1 . ASN A 288 ? 0.7404 0.8122 0.8605 -0.0438 -0.0256 -0.0082 289 ASN A OD1 
2309 N ND2 . ASN A 288 ? 0.7483 0.8258 0.8432 -0.0357 -0.0374 -0.0133 289 ASN A ND2 
2310 N N   . SER A 289 ? 0.5025 0.6363 0.6931 -0.0495 -0.0606 -0.0169 290 SER A N   
2311 C CA  . SER A 289 ? 0.4758 0.6248 0.7002 -0.0560 -0.0655 -0.0185 290 SER A CA  
2312 C C   . SER A 289 ? 0.4768 0.6310 0.7220 -0.0583 -0.0508 -0.0084 290 SER A C   
2313 O O   . SER A 289 ? 0.4102 0.5596 0.6421 -0.0527 -0.0390 -0.0002 290 SER A O   
2314 C CB  . SER A 289 ? 0.4353 0.6012 0.6651 -0.0512 -0.0777 -0.0209 290 SER A CB  
2315 O OG  . SER A 289 ? 0.4179 0.5910 0.6435 -0.0434 -0.0702 -0.0117 290 SER A OG  
2316 N N   . GLU A 290 ? 0.4278 0.5917 0.7062 -0.0667 -0.0517 -0.0092 291 GLU A N   
2317 C CA  . GLU A 290 ? 0.4238 0.5950 0.7250 -0.0687 -0.0373 0.0009  291 GLU A CA  
2318 C C   . GLU A 290 ? 0.4155 0.6006 0.7166 -0.0598 -0.0333 0.0081  291 GLU A C   
2319 O O   . GLU A 290 ? 0.4270 0.6106 0.7266 -0.0559 -0.0187 0.0176  291 GLU A O   
2320 C CB  . GLU A 290 ? 0.4765 0.6585 0.8171 -0.0797 -0.0403 -0.0018 291 GLU A CB  
2321 C CG  . GLU A 290 ? 0.5602 0.7483 0.9268 -0.0830 -0.0237 0.0091  291 GLU A CG  
2322 C CD  . GLU A 290 ? 0.5444 0.7548 0.9287 -0.0774 -0.0206 0.0157  291 GLU A CD  
2323 O OE1 . GLU A 290 ? 0.5091 0.7174 0.8815 -0.0696 -0.0070 0.0253  291 GLU A OE1 
2324 O OE2 . GLU A 290 ? 0.5314 0.7610 0.9410 -0.0803 -0.0324 0.0109  291 GLU A OE2 
2325 N N   . GLN A 291 ? 0.3938 0.5910 0.6940 -0.0554 -0.0464 0.0036  292 GLN A N   
2326 C CA  . GLN A 291 ? 0.3825 0.5919 0.6819 -0.0461 -0.0437 0.0100  292 GLN A CA  
2327 C C   . GLN A 291 ? 0.3766 0.5714 0.6433 -0.0377 -0.0338 0.0157  292 GLN A C   
2328 O O   . GLN A 291 ? 0.3640 0.5616 0.6320 -0.0323 -0.0224 0.0241  292 GLN A O   
2329 C CB  . GLN A 291 ? 0.3513 0.5733 0.6513 -0.0422 -0.0609 0.0035  292 GLN A CB  
2330 C CG  . GLN A 291 ? 0.3749 0.6057 0.6674 -0.0309 -0.0594 0.0096  292 GLN A CG  
2331 C CD  . GLN A 291 ? 0.3982 0.6481 0.7229 -0.0300 -0.0517 0.0167  292 GLN A CD  
2332 O OE1 . GLN A 291 ? 0.3993 0.6484 0.7175 -0.0227 -0.0398 0.0251  292 GLN A OE1 
2333 N NE2 . GLN A 291 ? 0.3654 0.6327 0.7256 -0.0372 -0.0586 0.0132  292 GLN A NE2 
2334 N N   . ILE A 292 ? 0.3815 0.5604 0.6190 -0.0363 -0.0380 0.0111  293 ILE A N   
2335 C CA  . ILE A 292 ? 0.3607 0.5263 0.5691 -0.0293 -0.0299 0.0157  293 ILE A CA  
2336 C C   . ILE A 292 ? 0.4072 0.5619 0.6139 -0.0315 -0.0155 0.0213  293 ILE A C   
2337 O O   . ILE A 292 ? 0.3793 0.5297 0.5749 -0.0256 -0.0057 0.0277  293 ILE A O   
2338 C CB  . ILE A 292 ? 0.3665 0.5202 0.5469 -0.0273 -0.0382 0.0095  293 ILE A CB  
2339 C CG1 . ILE A 292 ? 0.4308 0.5938 0.6073 -0.0223 -0.0510 0.0059  293 ILE A CG1 
2340 C CG2 . ILE A 292 ? 0.3885 0.5275 0.5422 -0.0224 -0.0292 0.0137  293 ILE A CG2 
2341 C CD1 . ILE A 292 ? 0.3756 0.5446 0.5473 -0.0134 -0.0476 0.0126  293 ILE A CD1 
2342 N N   . PHE A 293 ? 0.4063 0.5556 0.6235 -0.0395 -0.0143 0.0187  294 PHE A N   
2343 C CA  . PHE A 293 ? 0.4387 0.5750 0.6500 -0.0406 -0.0013 0.0239  294 PHE A CA  
2344 C C   . PHE A 293 ? 0.4323 0.5760 0.6609 -0.0393 0.0116  0.0331  294 PHE A C   
2345 O O   . PHE A 293 ? 0.4155 0.5499 0.6304 -0.0347 0.0229  0.0393  294 PHE A O   
2346 C CB  . PHE A 293 ? 0.4754 0.6022 0.6926 -0.0490 -0.0034 0.0189  294 PHE A CB  
2347 C CG  . PHE A 293 ? 0.5427 0.6558 0.7546 -0.0497 0.0096  0.0248  294 PHE A CG  
2348 C CD1 . PHE A 293 ? 0.5337 0.6329 0.7174 -0.0440 0.0136  0.0260  294 PHE A CD1 
2349 C CD2 . PHE A 293 ? 0.5427 0.6568 0.7781 -0.0556 0.0181  0.0294  294 PHE A CD2 
2350 C CE1 . PHE A 293 ? 0.5389 0.6256 0.7163 -0.0434 0.0247  0.0314  294 PHE A CE1 
2351 C CE2 . PHE A 293 ? 0.5398 0.6400 0.7680 -0.0550 0.0305  0.0356  294 PHE A CE2 
2352 C CZ  . PHE A 293 ? 0.5363 0.6227 0.7345 -0.0484 0.0333  0.0365  294 PHE A CZ  
2353 N N   . MET A 294 ? 0.4521 0.6128 0.7107 -0.0426 0.0101  0.0341  295 MET A N   
2354 C CA  . MET A 294 ? 0.4395 0.6071 0.7192 -0.0430 0.0238  0.0430  295 MET A CA  
2355 C C   . MET A 294 ? 0.4223 0.6069 0.7138 -0.0362 0.0265  0.0479  295 MET A C   
2356 O O   . MET A 294 ? 0.3890 0.5767 0.6897 -0.0332 0.0406  0.0565  295 MET A O   
2357 C CB  . MET A 294 ? 0.4778 0.6513 0.7900 -0.0542 0.0236  0.0417  295 MET A CB  
2358 C CG  . MET A 294 ? 0.5903 0.7454 0.8965 -0.0594 0.0317  0.0433  295 MET A CG  
2359 S SD  . MET A 294 ? 0.7314 0.8819 1.0406 -0.0553 0.0544  0.0573  295 MET A SD  
2360 C CE  . MET A 294 ? 0.5873 0.7630 0.9435 -0.0606 0.0583  0.0617  295 MET A CE  
2361 N N   . LYS A 295 ? 0.3440 0.5389 0.6345 -0.0327 0.0142  0.0432  296 LYS A N   
2362 C CA  . LYS A 295 ? 0.3587 0.5714 0.6646 -0.0264 0.0153  0.0473  296 LYS A CA  
2363 C C   . LYS A 295 ? 0.3119 0.5176 0.5890 -0.0151 0.0165  0.0494  296 LYS A C   
2364 O O   . LYS A 295 ? 0.2609 0.4511 0.5089 -0.0134 0.0125  0.0459  296 LYS A O   
2365 C CB  . LYS A 295 ? 0.3520 0.5833 0.6812 -0.0301 -0.0004 0.0408  296 LYS A CB  
2366 C CG  . LYS A 295 ? 0.4351 0.6747 0.7970 -0.0421 -0.0032 0.0376  296 LYS A CG  
2367 C CD  . LYS A 295 ? 0.4474 0.6959 0.8377 -0.0445 0.0131  0.0470  296 LYS A CD  
2368 C CE  . LYS A 295 ? 0.4077 0.6666 0.8356 -0.0575 0.0095  0.0438  296 LYS A CE  
2369 N NZ  . LYS A 295 ? 0.3983 0.6761 0.8471 -0.0604 -0.0095 0.0351  296 LYS A NZ  
2370 N N   . PRO A 296 ? 0.2690 0.4852 0.5541 -0.0071 0.0228  0.0553  297 PRO A N   
2371 C CA  . PRO A 296 ? 0.2146 0.4234 0.4737 0.0036  0.0230  0.0567  297 PRO A CA  
2372 C C   . PRO A 296 ? 0.2094 0.4259 0.4667 0.0060  0.0075  0.0514  297 PRO A C   
2373 O O   . PRO A 296 ? 0.2148 0.4505 0.4978 0.0053  0.0006  0.0504  297 PRO A O   
2374 C CB  . PRO A 296 ? 0.2550 0.4726 0.5262 0.0114  0.0358  0.0648  297 PRO A CB  
2375 C CG  . PRO A 296 ? 0.2019 0.4313 0.5049 0.0044  0.0439  0.0686  297 PRO A CG  
2376 C CD  . PRO A 296 ? 0.2665 0.5006 0.5845 -0.0071 0.0316  0.0615  297 PRO A CD  
2377 N N   . ASN A 297 ? 0.1804 0.3824 0.4080 0.0091  0.0021  0.0483  298 ASN A N   
2378 C CA  . ASN A 297 ? 0.1830 0.3888 0.4032 0.0125  -0.0115 0.0441  298 ASN A CA  
2379 C C   . ASN A 297 ? 0.1858 0.3824 0.3832 0.0229  -0.0088 0.0476  298 ASN A C   
2380 O O   . ASN A 297 ? 0.1858 0.3653 0.3607 0.0243  -0.0019 0.0489  298 ASN A O   
2381 C CB  . ASN A 297 ? 0.2342 0.4305 0.4401 0.0062  -0.0213 0.0368  298 ASN A CB  
2382 C CG  . ASN A 297 ? 0.2796 0.4843 0.5085 -0.0039 -0.0262 0.0321  298 ASN A CG  
2383 O OD1 . ASN A 297 ? 0.2930 0.5127 0.5409 -0.0057 -0.0371 0.0282  298 ASN A OD1 
2384 N ND2 . ASN A 297 ? 0.2872 0.4816 0.5150 -0.0104 -0.0183 0.0324  298 ASN A ND2 
2385 N N   . LYS A 298 ? 0.1895 0.3973 0.3934 0.0301  -0.0150 0.0488  299 LYS A N   
2386 C CA  . LYS A 298 ? 0.1948 0.3931 0.3781 0.0403  -0.0134 0.0520  299 LYS A CA  
2387 C C   . LYS A 298 ? 0.1978 0.3779 0.3512 0.0393  -0.0181 0.0489  299 LYS A C   
2388 O O   . LYS A 298 ? 0.1997 0.3813 0.3495 0.0357  -0.0286 0.0441  299 LYS A O   
2389 C CB  . LYS A 298 ? 0.1998 0.4144 0.3967 0.0481  -0.0211 0.0535  299 LYS A CB  
2390 C CG  . LYS A 298 ? 0.2305 0.4350 0.4075 0.0595  -0.0197 0.0573  299 LYS A CG  
2391 C CD  . LYS A 298 ? 0.2180 0.4154 0.3922 0.0651  -0.0055 0.0626  299 LYS A CD  
2392 C CE  . LYS A 298 ? 0.3166 0.5105 0.4817 0.0779  -0.0052 0.0667  299 LYS A CE  
2393 N NZ  . LYS A 298 ? 0.4506 0.6672 0.6395 0.0837  -0.0126 0.0681  299 LYS A NZ  
2394 N N   . VAL A 299 ? 0.1998 0.3627 0.3318 0.0429  -0.0103 0.0514  300 VAL A N   
2395 C CA  . VAL A 299 ? 0.2032 0.3493 0.3090 0.0422  -0.0129 0.0495  300 VAL A CA  
2396 C C   . VAL A 299 ? 0.2129 0.3550 0.3067 0.0512  -0.0167 0.0523  300 VAL A C   
2397 O O   . VAL A 299 ? 0.2170 0.3646 0.3181 0.0591  -0.0145 0.0562  300 VAL A O   
2398 C CB  . VAL A 299 ? 0.2009 0.3302 0.2914 0.0397  -0.0034 0.0499  300 VAL A CB  
2399 C CG1 . VAL A 299 ? 0.1940 0.3273 0.2973 0.0337  0.0027  0.0493  300 VAL A CG1 
2400 C CG2 . VAL A 299 ? 0.2072 0.3266 0.2874 0.0477  0.0035  0.0538  300 VAL A CG2 
2401 N N   . THR A 300 ? 0.2183 0.3502 0.2930 0.0507  -0.0219 0.0508  301 THR A N   
2402 C CA  . THR A 300 ? 0.2352 0.3592 0.2949 0.0590  -0.0241 0.0543  301 THR A CA  
2403 C C   . THR A 300 ? 0.2720 0.3753 0.3088 0.0571  -0.0191 0.0550  301 THR A C   
2404 O O   . THR A 300 ? 0.2333 0.3315 0.2634 0.0498  -0.0190 0.0516  301 THR A O   
2405 C CB  . THR A 300 ? 0.2650 0.3978 0.3238 0.0621  -0.0360 0.0530  301 THR A CB  
2406 O OG1 . THR A 300 ? 0.3794 0.5078 0.4282 0.0553  -0.0401 0.0485  301 THR A OG1 
2407 C CG2 . THR A 300 ? 0.2342 0.3892 0.3189 0.0628  -0.0426 0.0514  301 THR A CG2 
2408 N N   . ALA A 301 ? 0.2838 0.3752 0.3098 0.0636  -0.0147 0.0592  302 ALA A N   
2409 C CA  . ALA A 301 ? 0.3345 0.4065 0.3415 0.0613  -0.0102 0.0599  302 ALA A CA  
2410 C C   . ALA A 301 ? 0.3423 0.4108 0.3365 0.0595  -0.0153 0.0597  302 ALA A C   
2411 O O   . ALA A 301 ? 0.3152 0.3914 0.3089 0.0642  -0.0226 0.0606  302 ALA A O   
2412 C CB  . ALA A 301 ? 0.3840 0.4428 0.3825 0.0689  -0.0054 0.0643  302 ALA A CB  
2413 N N   . ILE A 302 ? 0.3721 0.4291 0.3555 0.0533  -0.0115 0.0585  303 ILE A N   
2414 C CA  . ILE A 302 ? 0.4093 0.4621 0.3797 0.0518  -0.0142 0.0587  303 ILE A CA  
2415 C C   . ILE A 302 ? 0.5159 0.5553 0.4714 0.0581  -0.0121 0.0649  303 ILE A C   
2416 O O   . ILE A 302 ? 0.5847 0.6113 0.5368 0.0586  -0.0059 0.0675  303 ILE A O   
2417 C CB  . ILE A 302 ? 0.4712 0.5186 0.4384 0.0430  -0.0102 0.0553  303 ILE A CB  
2418 C CG1 . ILE A 302 ? 0.3601 0.4200 0.3397 0.0376  -0.0133 0.0497  303 ILE A CG1 
2419 C CG2 . ILE A 302 ? 0.4722 0.5119 0.4240 0.0425  -0.0098 0.0572  303 ILE A CG2 
2420 C CD1 . ILE A 302 ? 0.3339 0.3892 0.3127 0.0301  -0.0088 0.0466  303 ILE A CD1 
2421 N N   . SER A 303 ? 0.6063 0.6474 0.5520 0.0633  -0.0175 0.0672  304 SER A N   
2422 C CA  . SER A 303 ? 0.7174 0.7444 0.6466 0.0697  -0.0149 0.0741  304 SER A CA  
2423 C C   . SER A 303 ? 0.7260 0.7395 0.6443 0.0633  -0.0075 0.0755  304 SER A C   
2424 O O   . SER A 303 ? 0.7425 0.7424 0.6590 0.0612  -0.0003 0.0782  304 SER A O   
2425 C CB  . SER A 303 ? 0.7569 0.7902 0.6770 0.0781  -0.0232 0.0762  304 SER A CB  
2426 O OG  . SER A 303 ? 0.8414 0.8779 0.7537 0.0745  -0.0262 0.0728  304 SER A OG  
2427 N N   . LYS A 304 ? 0.6558 0.6731 0.5675 0.0605  -0.0094 0.0733  305 LYS A N   
2428 C CA  . LYS A 304 ? 0.6936 0.7034 0.6004 0.0531  -0.0026 0.0729  305 LYS A CA  
2429 C C   . LYS A 304 ? 0.5991 0.6206 0.5116 0.0476  -0.0064 0.0657  305 LYS A C   
2430 O O   . LYS A 304 ? 0.5804 0.6127 0.4938 0.0506  -0.0146 0.0622  305 LYS A O   
2431 C CB  . LYS A 304 ? 0.7443 0.7422 0.6326 0.0570  0.0020  0.0799  305 LYS A CB  
2432 C CG  . LYS A 304 ? 0.7616 0.7648 0.6359 0.0646  -0.0047 0.0806  305 LYS A CG  
2433 C CD  . LYS A 304 ? 0.8466 0.8368 0.7007 0.0685  0.0021  0.0881  305 LYS A CD  
2434 C CE  . LYS A 304 ? 0.8890 0.8766 0.7433 0.0602  0.0101  0.0868  305 LYS A CE  
2435 N NZ  . LYS A 304 ? 0.8967 0.8721 0.7326 0.0639  0.0187  0.0951  305 LYS A NZ  
2436 N N   . GLU A 305 ? 0.5668 0.5862 0.4842 0.0395  -0.0010 0.0630  306 GLU A N   
2437 C CA  A GLU A 305 ? 0.5100 0.5384 0.4320 0.0347  -0.0036 0.0565  306 GLU A CA  
2438 C CA  B GLU A 305 ? 0.5128 0.5409 0.4346 0.0345  -0.0034 0.0566  306 GLU A CA  
2439 C C   . GLU A 305 ? 0.4919 0.5206 0.3991 0.0382  -0.0058 0.0566  306 GLU A C   
2440 O O   . GLU A 305 ? 0.4835 0.5035 0.3762 0.0427  -0.0022 0.0627  306 GLU A O   
2441 C CB  A GLU A 305 ? 0.5138 0.5392 0.4426 0.0268  0.0027  0.0545  306 GLU A CB  
2442 C CB  B GLU A 305 ? 0.5149 0.5394 0.4427 0.0268  0.0033  0.0549  306 GLU A CB  
2443 C CG  A GLU A 305 ? 0.4340 0.4682 0.3762 0.0221  0.0000  0.0480  306 GLU A CG  
2444 C CG  B GLU A 305 ? 0.4809 0.5007 0.4181 0.0240  0.0065  0.0554  306 GLU A CG  
2445 C CD  A GLU A 305 ? 0.4264 0.4573 0.3751 0.0159  0.0053  0.0464  306 GLU A CD  
2446 C CD  B GLU A 305 ? 0.4132 0.4414 0.3628 0.0228  0.0029  0.0507  306 GLU A CD  
2447 O OE1 A GLU A 305 ? 0.4496 0.4725 0.3987 0.0151  0.0092  0.0492  306 GLU A OE1 
2448 O OE1 B GLU A 305 ? 0.3849 0.4229 0.3383 0.0228  -0.0020 0.0471  306 GLU A OE1 
2449 O OE2 A GLU A 305 ? 0.3846 0.4204 0.3376 0.0121  0.0049  0.0421  306 GLU A OE2 
2450 O OE2 B GLU A 305 ? 0.3789 0.4031 0.3340 0.0220  0.0052  0.0507  306 GLU A OE2 
2451 N N   . PRO A 306 ? 0.4599 0.4973 0.3692 0.0368  -0.0117 0.0501  307 PRO A N   
2452 C CA  . PRO A 306 ? 0.4510 0.4873 0.3439 0.0407  -0.0140 0.0490  307 PRO A CA  
2453 C C   . PRO A 306 ? 0.4578 0.4858 0.3421 0.0384  -0.0038 0.0523  307 PRO A C   
2454 O O   . PRO A 306 ? 0.4542 0.4813 0.3491 0.0317  0.0023  0.0519  307 PRO A O   
2455 C CB  . PRO A 306 ? 0.4433 0.4891 0.3440 0.0375  -0.0216 0.0400  307 PRO A CB  
2456 C CG  . PRO A 306 ? 0.4532 0.5030 0.3735 0.0303  -0.0192 0.0377  307 PRO A CG  
2457 C CD  . PRO A 306 ? 0.4667 0.5140 0.3924 0.0319  -0.0164 0.0434  307 PRO A CD  
2458 N N   . SER A 307 ? 0.4297 0.4520 0.2946 0.0446  -0.0020 0.0559  308 SER A N   
2459 C CA  . SER A 307 ? 0.4664 0.4809 0.3235 0.0434  0.0094  0.0609  308 SER A CA  
2460 C C   . SER A 307 ? 0.4795 0.4984 0.3408 0.0385  0.0119  0.0550  308 SER A C   
2461 O O   . SER A 307 ? 0.4734 0.4904 0.3412 0.0336  0.0210  0.0573  308 SER A O   
2462 C CB  . SER A 307 ? 0.5343 0.5409 0.3675 0.0527  0.0117  0.0673  308 SER A CB  
2463 O OG  . SER A 307 ? 0.6580 0.6580 0.4843 0.0517  0.0239  0.0727  308 SER A OG  
2464 N N   . VAL A 308 ? 0.4200 0.4446 0.2784 0.0399  0.0037  0.0472  309 VAL A N   
2465 C CA  . VAL A 308 ? 0.4198 0.4473 0.2809 0.0366  0.0052  0.0410  309 VAL A CA  
2466 C C   . VAL A 308 ? 0.3635 0.3985 0.2398 0.0320  -0.0037 0.0330  309 VAL A C   
2467 O O   . VAL A 308 ? 0.3133 0.3520 0.1895 0.0345  -0.0135 0.0297  309 VAL A O   
2468 C CB  . VAL A 308 ? 0.4834 0.5072 0.3224 0.0437  0.0052  0.0392  309 VAL A CB  
2469 C CG1 . VAL A 308 ? 0.4530 0.4778 0.2943 0.0408  0.0105  0.0348  309 VAL A CG1 
2470 C CG2 . VAL A 308 ? 0.4836 0.4992 0.3045 0.0503  0.0132  0.0487  309 VAL A CG2 
2471 N N   . LYS A 309 ? 0.4329 0.2867 0.2720 0.0414  -0.0262 0.0478  310 LYS A N   
2472 C CA  . LYS A 309 ? 0.4009 0.2761 0.2558 0.0448  -0.0309 0.0390  310 LYS A CA  
2473 C C   . LYS A 309 ? 0.4330 0.3217 0.2963 0.0383  -0.0219 0.0354  310 LYS A C   
2474 O O   . LYS A 309 ? 0.4282 0.3117 0.2910 0.0313  -0.0122 0.0379  310 LYS A O   
2475 C CB  . LYS A 309 ? 0.4542 0.3331 0.3272 0.0487  -0.0352 0.0354  310 LYS A CB  
2476 C CG  . LYS A 309 ? 0.5615 0.4293 0.4304 0.0570  -0.0466 0.0364  310 LYS A CG  
2477 C CD  . LYS A 309 ? 0.5690 0.4180 0.4429 0.0539  -0.0450 0.0410  310 LYS A CD  
2478 C CE  . LYS A 309 ? 0.5864 0.4293 0.4664 0.0634  -0.0579 0.0379  310 LYS A CE  
2479 N NZ  . LYS A 309 ? 0.6286 0.4444 0.5030 0.0610  -0.0595 0.0461  310 LYS A NZ  
2480 N N   . MET A 310 ? 0.3814 0.2878 0.2535 0.0407  -0.0254 0.0294  311 MET A N   
2481 C CA  . MET A 310 ? 0.3660 0.2855 0.2510 0.0357  -0.0189 0.0257  311 MET A CA  
2482 C C   . MET A 310 ? 0.3325 0.2684 0.2330 0.0404  -0.0227 0.0214  311 MET A C   
2483 O O   . MET A 310 ? 0.3580 0.2980 0.2593 0.0475  -0.0305 0.0202  311 MET A O   
2484 C CB  . MET A 310 ? 0.4153 0.3388 0.2933 0.0324  -0.0171 0.0239  311 MET A CB  
2485 C CG  . MET A 310 ? 0.4197 0.3519 0.2963 0.0375  -0.0264 0.0207  311 MET A CG  
2486 S SD  . MET A 310 ? 0.6183 0.5546 0.4898 0.0341  -0.0261 0.0165  311 MET A SD  
2487 C CE  . MET A 310 ? 0.4733 0.4275 0.3698 0.0292  -0.0225 0.0126  311 MET A CE  
2488 N N   . TYR A 311 ? 0.3174 0.2630 0.2297 0.0370  -0.0170 0.0193  312 TYR A N   
2489 C CA  . TYR A 311 ? 0.3043 0.2634 0.2294 0.0417  -0.0179 0.0170  312 TYR A CA  
2490 C C   . TYR A 311 ? 0.2937 0.2641 0.2269 0.0372  -0.0128 0.0161  312 TYR A C   
2491 O O   . TYR A 311 ? 0.2934 0.2583 0.2252 0.0309  -0.0077 0.0160  312 TYR A O   
2492 C CB  . TYR A 311 ? 0.3008 0.2546 0.2316 0.0441  -0.0163 0.0160  312 TYR A CB  
2493 C CG  . TYR A 311 ? 0.3123 0.2526 0.2389 0.0475  -0.0213 0.0169  312 TYR A CG  
2494 C CD1 . TYR A 311 ? 0.3245 0.2485 0.2441 0.0414  -0.0179 0.0205  312 TYR A CD1 
2495 C CD2 . TYR A 311 ? 0.3221 0.2656 0.2521 0.0568  -0.0291 0.0145  312 TYR A CD2 
2496 C CE1 . TYR A 311 ? 0.3734 0.2829 0.2906 0.0435  -0.0222 0.0228  312 TYR A CE1 
2497 C CE2 . TYR A 311 ? 0.3837 0.3128 0.3114 0.0600  -0.0350 0.0151  312 TYR A CE2 
2498 C CZ  . TYR A 311 ? 0.3516 0.2627 0.2735 0.0527  -0.0315 0.0198  312 TYR A CZ  
2499 O OH  . TYR A 311 ? 0.3822 0.2773 0.3033 0.0552  -0.0373 0.0217  312 TYR A OH  
2500 N N   . HIS A 312 ? 0.2866 0.2725 0.2290 0.0405  -0.0138 0.0156  313 HIS A N   
2501 C CA  . HIS A 312 ? 0.2786 0.2729 0.2300 0.0359  -0.0081 0.0165  313 HIS A CA  
2502 C C   . HIS A 312 ? 0.2724 0.2820 0.2329 0.0417  -0.0065 0.0178  313 HIS A C   
2503 O O   . HIS A 312 ? 0.2735 0.2898 0.2339 0.0497  -0.0104 0.0168  313 HIS A O   
2504 C CB  . HIS A 312 ? 0.2810 0.2780 0.2349 0.0294  -0.0090 0.0156  313 HIS A CB  
2505 C CG  . HIS A 312 ? 0.3064 0.3179 0.2689 0.0315  -0.0134 0.0147  313 HIS A CG  
2506 N ND1 . HIS A 312 ? 0.2947 0.3098 0.2625 0.0268  -0.0165 0.0121  313 HIS A ND1 
2507 C CD2 . HIS A 312 ? 0.3083 0.3330 0.2770 0.0381  -0.0156 0.0147  313 HIS A CD2 
2508 C CE1 . HIS A 312 ? 0.3254 0.3554 0.3040 0.0298  -0.0203 0.0107  313 HIS A CE1 
2509 N NE2 . HIS A 312 ? 0.3035 0.3403 0.2825 0.0367  -0.0193 0.0124  313 HIS A NE2 
2510 N N   . LYS A 313 ? 0.2680 0.2828 0.2353 0.0382  -0.0004 0.0204  314 LYS A N   
2511 C CA  . LYS A 313 ? 0.2655 0.2954 0.2401 0.0428  0.0035  0.0237  314 LYS A CA  
2512 C C   . LYS A 313 ? 0.2648 0.2987 0.2488 0.0348  0.0094  0.0280  314 LYS A C   
2513 O O   . LYS A 313 ? 0.2651 0.2874 0.2473 0.0292  0.0111  0.0279  314 LYS A O   
2514 C CB  . LYS A 313 ? 0.2653 0.2930 0.2342 0.0515  0.0050  0.0236  314 LYS A CB  
2515 C CG  . LYS A 313 ? 0.2664 0.3105 0.2386 0.0589  0.0097  0.0275  314 LYS A CG  
2516 C CD  . LYS A 313 ? 0.3103 0.3681 0.2843 0.0672  0.0054  0.0249  314 LYS A CD  
2517 C CE  . LYS A 313 ? 0.3715 0.4490 0.3489 0.0750  0.0115  0.0287  314 LYS A CE  
2518 N NZ  . LYS A 313 ? 0.3993 0.4897 0.3898 0.0662  0.0194  0.0353  314 LYS A NZ  
2519 N N   . THR A 314 ? 0.2682 0.3186 0.2640 0.0343  0.0123  0.0313  315 THR A N   
2520 C CA  . THR A 314 ? 0.3548 0.4090 0.3624 0.0265  0.0186  0.0369  315 THR A CA  
2521 C C   . THR A 314 ? 0.4238 0.4844 0.4296 0.0321  0.0269  0.0442  315 THR A C   
2522 O O   . THR A 314 ? 0.3225 0.3933 0.3234 0.0422  0.0278  0.0443  315 THR A O   
2523 C CB  . THR A 314 ? 0.4414 0.5098 0.4668 0.0207  0.0175  0.0366  315 THR A CB  
2524 O OG1 . THR A 314 ? 0.4612 0.5489 0.4921 0.0278  0.0193  0.0376  315 THR A OG1 
2525 C CG2 . THR A 314 ? 0.4592 0.5203 0.4823 0.0179  0.0080  0.0287  315 THR A CG2 
2526 N N   . GLY A 315 ? 0.4265 0.4803 0.4350 0.0265  0.0324  0.0499  316 GLY A N   
2527 C CA  . GLY A 315 ? 0.4723 0.5279 0.4749 0.0324  0.0403  0.0579  316 GLY A CA  
2528 C C   . GLY A 315 ? 0.6563 0.7220 0.6736 0.0255  0.0492  0.0680  316 GLY A C   
2529 O O   . GLY A 315 ? 0.5990 0.6561 0.6143 0.0232  0.0549  0.0758  316 GLY A O   
2530 N N   . THR A 316 ? 1.0156 1.0997 1.0489 0.0224  0.0502  0.0678  317 THR A N   
2531 C CA  . THR A 316 ? 1.0985 1.1963 1.1536 0.0137  0.0582  0.0759  317 THR A CA  
2532 C C   . THR A 316 ? 1.1204 1.2172 1.1728 0.0140  0.0705  0.0896  317 THR A C   
2533 O O   . THR A 316 ? 1.0748 1.1541 1.1264 0.0076  0.0714  0.0942  317 THR A O   
2534 C CB  . THR A 316 ? 1.1343 1.2575 1.2017 0.0174  0.0592  0.0734  317 THR A CB  
2535 O OG1 . THR A 316 ? 1.1386 1.2739 1.1939 0.0299  0.0667  0.0783  317 THR A OG1 
2536 C CG2 . THR A 316 ? 1.0412 1.1623 1.1040 0.0209  0.0464  0.0605  317 THR A CG2 
2537 N N   . THR A 317 ? 0.9871 1.1027 1.0372 0.0222  0.0799  0.0963  318 THR A N   
2538 C CA  . THR A 317 ? 0.9614 1.0789 1.0066 0.0242  0.0936  0.1112  318 THR A CA  
2539 C C   . THR A 317 ? 0.9915 1.1017 1.0567 0.0084  0.0994  0.1211  318 THR A C   
2540 O O   . THR A 317 ? 1.0296 1.1488 1.1219 -0.0035 0.0978  0.1186  318 THR A O   
2541 C CB  . THR A 317 ? 0.8640 0.9635 0.8794 0.0364  0.0920  0.1121  318 THR A CB  
2542 O OG1 . THR A 317 ? 0.7702 0.8446 0.7822 0.0298  0.0836  0.1076  318 THR A OG1 
2543 C CG2 . THR A 317 ? 0.7379 0.8437 0.7365 0.0519  0.0849  0.1012  318 THR A CG2 
2544 N N   . ASN A 318 ? 0.9693 1.0627 1.0220 0.0088  0.1053  0.1320  319 ASN A N   
2545 C CA  . ASN A 318 ? 0.9379 1.0170 1.0068 -0.0057 0.1080  0.1405  319 ASN A CA  
2546 C C   . ASN A 318 ? 0.8777 0.9297 0.9223 -0.0003 0.1062  0.1447  319 ASN A C   
2547 O O   . ASN A 318 ? 0.8716 0.9185 0.8896 0.0141  0.1030  0.1404  319 ASN A O   
2548 C CB  . ASN A 318 ? 0.9663 1.0624 1.0574 -0.0141 0.1238  0.1562  319 ASN A CB  
2549 C CG  . ASN A 318 ? 0.9853 1.0855 1.0552 -0.0033 0.1388  0.1720  319 ASN A CG  
2550 O OD1 . ASN A 318 ? 1.0142 1.1149 1.0555 0.0134  0.1372  0.1683  319 ASN A OD1 
2551 N ND2 . ASN A 318 ? 0.9645 1.0674 1.0487 -0.0123 0.1535  0.1898  319 ASN A ND2 
2552 N N   . ARG A 319 ? 0.8766 0.9108 0.9319 -0.0116 0.1067  0.1518  320 ARG A N   
2553 C CA  . ARG A 319 ? 0.8051 0.8112 0.8413 -0.0081 0.1026  0.1542  320 ARG A CA  
2554 C C   . ARG A 319 ? 0.7978 0.7914 0.8210 -0.0024 0.0875  0.1364  320 ARG A C   
2555 O O   . ARG A 319 ? 0.7812 0.7535 0.7877 0.0028  0.0826  0.1352  320 ARG A O   
2556 C CB  . ARG A 319 ? 0.8143 0.8171 0.8235 0.0053  0.1128  0.1675  320 ARG A CB  
2557 C CG  . ARG A 319 ? 0.8601 0.8742 0.8793 0.0002  0.1304  0.1878  320 ARG A CG  
2558 C CD  . ARG A 319 ? 0.9604 0.9949 0.9598 0.0158  0.1408  0.1932  320 ARG A CD  
2559 N NE  . ARG A 319 ? 1.0357 1.0588 1.0007 0.0346  0.1333  0.1858  320 ARG A NE  
2560 C CZ  . ARG A 319 ? 1.0363 1.0704 0.9769 0.0521  0.1396  0.1893  320 ARG A CZ  
2561 N NH1 . ARG A 319 ? 1.0400 1.0972 0.9841 0.0540  0.1552  0.2015  320 ARG A NH1 
2562 N NH2 . ARG A 319 ? 0.9367 0.9592 0.8498 0.0687  0.1297  0.1796  320 ARG A NH2 
2563 N N   . SER A 320 ? 0.6700 0.6761 0.7005 -0.0031 0.0803  0.1229  321 SER A N   
2564 C CA  . SER A 320 ? 0.5973 0.5927 0.6181 0.0004  0.0677  0.1072  321 SER A CA  
2565 C C   . SER A 320 ? 0.5509 0.5601 0.5858 -0.0046 0.0616  0.0961  321 SER A C   
2566 O O   . SER A 320 ? 0.5849 0.6141 0.6312 -0.0058 0.0662  0.0987  321 SER A O   
2567 C CB  . SER A 320 ? 0.6007 0.5932 0.5954 0.0163  0.0660  0.1032  321 SER A CB  
2568 O OG  . SER A 320 ? 0.6262 0.6390 0.6171 0.0243  0.0695  0.1026  321 SER A OG  
2569 N N   . GLY A 321 ? 0.4432 0.4413 0.4766 -0.0069 0.0512  0.0839  322 GLY A N   
2570 C CA  . GLY A 321 ? 0.4170 0.4240 0.4554 -0.0083 0.0443  0.0727  322 GLY A CA  
2571 C C   . GLY A 321 ? 0.4553 0.4534 0.4746 -0.0001 0.0384  0.0631  322 GLY A C   
2572 O O   . GLY A 321 ? 0.4239 0.4061 0.4348 0.0011  0.0358  0.0606  322 GLY A O   
2573 N N   . THR A 322 ? 0.3568 0.3650 0.3702 0.0058  0.0362  0.0579  323 THR A N   
2574 C CA  . THR A 322 ? 0.3229 0.3236 0.3220 0.0122  0.0310  0.0492  323 THR A CA  
2575 C C   . THR A 322 ? 0.2930 0.3005 0.2943 0.0108  0.0257  0.0423  323 THR A C   
2576 O O   . THR A 322 ? 0.3004 0.3223 0.3095 0.0109  0.0265  0.0443  323 THR A O   
2577 C CB  . THR A 322 ? 0.3592 0.3621 0.3448 0.0244  0.0335  0.0511  323 THR A CB  
2578 O OG1 . THR A 322 ? 0.3845 0.3821 0.3660 0.0270  0.0389  0.0592  323 THR A OG1 
2579 C CG2 . THR A 322 ? 0.3354 0.3281 0.3105 0.0295  0.0279  0.0417  323 THR A CG2 
2580 N N   . TYR A 323 ? 0.2837 0.2811 0.2782 0.0099  0.0206  0.0344  324 TYR A N   
2581 C CA  . TYR A 323 ? 0.2704 0.2709 0.2617 0.0105  0.0158  0.0289  324 TYR A CA  
2582 C C   . TYR A 323 ? 0.2690 0.2583 0.2483 0.0136  0.0139  0.0234  324 TYR A C   
2583 O O   . TYR A 323 ? 0.2706 0.2498 0.2479 0.0111  0.0143  0.0205  324 TYR A O   
2584 C CB  . TYR A 323 ? 0.2726 0.2739 0.2722 0.0030  0.0114  0.0255  324 TYR A CB  
2585 C CG  . TYR A 323 ? 0.2752 0.2784 0.2685 0.0051  0.0059  0.0205  324 TYR A CG  
2586 C CD1 . TYR A 323 ? 0.2983 0.3134 0.2937 0.0097  0.0044  0.0218  324 TYR A CD1 
2587 C CD2 . TYR A 323 ? 0.2926 0.2859 0.2769 0.0033  0.0020  0.0146  324 TYR A CD2 
2588 C CE1 . TYR A 323 ? 0.3009 0.3155 0.2889 0.0125  -0.0019 0.0175  324 TYR A CE1 
2589 C CE2 . TYR A 323 ? 0.2845 0.2774 0.2598 0.0060  -0.0029 0.0114  324 TYR A CE2 
2590 C CZ  . TYR A 323 ? 0.2976 0.3001 0.2747 0.0106  -0.0054 0.0129  324 TYR A CZ  
2591 O OH  . TYR A 323 ? 0.2865 0.2862 0.2530 0.0142  -0.0114 0.0101  324 TYR A OH  
2592 N N   . VAL A 324 ? 0.2672 0.2584 0.2400 0.0189  0.0117  0.0217  325 VAL A N   
2593 C CA  . VAL A 324 ? 0.2674 0.2485 0.2318 0.0205  0.0106  0.0173  325 VAL A CA  
2594 C C   . VAL A 324 ? 0.2705 0.2511 0.2292 0.0209  0.0066  0.0159  325 VAL A C   
2595 O O   . VAL A 324 ? 0.2704 0.2597 0.2308 0.0242  0.0039  0.0176  325 VAL A O   
2596 C CB  . VAL A 324 ? 0.2654 0.2453 0.2279 0.0284  0.0113  0.0168  325 VAL A CB  
2597 C CG1 . VAL A 324 ? 0.2831 0.2609 0.2477 0.0295  0.0144  0.0182  325 VAL A CG1 
2598 C CG2 . VAL A 324 ? 0.2824 0.2722 0.2446 0.0360  0.0094  0.0190  325 VAL A CG2 
2599 N N   . VAL A 325 ? 0.2750 0.2456 0.2266 0.0179  0.0067  0.0131  326 VAL A N   
2600 C CA  . VAL A 325 ? 0.2824 0.2491 0.2251 0.0186  0.0034  0.0131  326 VAL A CA  
2601 C C   . VAL A 325 ? 0.2877 0.2428 0.2236 0.0171  0.0066  0.0120  326 VAL A C   
2602 O O   . VAL A 325 ? 0.2975 0.2491 0.2352 0.0135  0.0109  0.0094  326 VAL A O   
2603 C CB  . VAL A 325 ? 0.2884 0.2571 0.2283 0.0152  0.0002  0.0118  326 VAL A CB  
2604 C CG1 . VAL A 325 ? 0.2977 0.2620 0.2375 0.0099  0.0028  0.0085  326 VAL A CG1 
2605 C CG2 . VAL A 325 ? 0.3000 0.2624 0.2266 0.0176  -0.0038 0.0122  326 VAL A CG2 
2606 N N   . PHE A 326 ? 0.2949 0.2439 0.2241 0.0196  0.0046  0.0140  327 PHE A N   
2607 C CA  . PHE A 326 ? 0.3030 0.2410 0.2271 0.0164  0.0091  0.0144  327 PHE A CA  
2608 C C   . PHE A 326 ? 0.3179 0.2471 0.2291 0.0176  0.0066  0.0186  327 PHE A C   
2609 O O   . PHE A 326 ? 0.3200 0.2510 0.2286 0.0226  -0.0002 0.0200  327 PHE A O   
2610 C CB  . PHE A 326 ? 0.2970 0.2329 0.2320 0.0177  0.0113  0.0123  327 PHE A CB  
2611 C CG  . PHE A 326 ? 0.2970 0.2317 0.2356 0.0240  0.0057  0.0132  327 PHE A CG  
2612 C CD1 . PHE A 326 ? 0.2883 0.2327 0.2324 0.0308  0.0012  0.0117  327 PHE A CD1 
2613 C CD2 . PHE A 326 ? 0.3080 0.2316 0.2449 0.0236  0.0051  0.0155  327 PHE A CD2 
2614 C CE1 . PHE A 326 ? 0.2894 0.2337 0.2364 0.0383  -0.0048 0.0108  327 PHE A CE1 
2615 C CE2 . PHE A 326 ? 0.3088 0.2302 0.2504 0.0302  -0.0018 0.0150  327 PHE A CE2 
2616 C CZ  . PHE A 326 ? 0.2994 0.2317 0.2456 0.0382  -0.0073 0.0117  327 PHE A CZ  
2617 N N   . ILE A 327 ? 0.3302 0.2501 0.2325 0.0135  0.0124  0.0207  328 ILE A N   
2618 C CA  . ILE A 327 ? 0.3597 0.2679 0.2457 0.0141  0.0120  0.0265  328 ILE A CA  
2619 C C   . ILE A 327 ? 0.4021 0.2998 0.2902 0.0099  0.0197  0.0303  328 ILE A C   
2620 O O   . ILE A 327 ? 0.3847 0.2815 0.2707 0.0049  0.0288  0.0302  328 ILE A O   
2621 C CB  . ILE A 327 ? 0.3913 0.2984 0.2600 0.0137  0.0127  0.0265  328 ILE A CB  
2622 C CG1 . ILE A 327 ? 0.4124 0.3310 0.2846 0.0164  0.0052  0.0213  328 ILE A CG1 
2623 C CG2 . ILE A 327 ? 0.4668 0.3603 0.3151 0.0164  0.0114  0.0334  328 ILE A CG2 
2624 C CD1 . ILE A 327 ? 0.4603 0.3804 0.3221 0.0155  0.0056  0.0176  328 ILE A CD1 
2625 N N   . PRO A 328 ? 0.3751 0.2653 0.2693 0.0118  0.0164  0.0331  329 PRO A N   
2626 C CA  . PRO A 328 ? 0.4330 0.3134 0.3349 0.0066  0.0236  0.0365  329 PRO A CA  
2627 C C   . PRO A 328 ? 0.4456 0.3155 0.3307 0.0018  0.0329  0.0443  329 PRO A C   
2628 O O   . PRO A 328 ? 0.4622 0.3318 0.3548 -0.0047 0.0436  0.0449  329 PRO A O   
2629 C CB  . PRO A 328 ? 0.4245 0.2968 0.3329 0.0112  0.0149  0.0382  329 PRO A CB  
2630 C CG  . PRO A 328 ? 0.4370 0.3221 0.3497 0.0188  0.0053  0.0319  329 PRO A CG  
2631 C CD  . PRO A 328 ? 0.3798 0.2728 0.2792 0.0190  0.0058  0.0315  329 PRO A CD  
2632 N N   . LYS A 329 ? 0.4498 0.3121 0.3120 0.0055  0.0290  0.0499  330 LYS A N   
2633 C CA  . LYS A 329 ? 0.5419 0.3931 0.3826 0.0030  0.0377  0.0584  330 LYS A CA  
2634 C C   . LYS A 329 ? 0.5496 0.4105 0.3885 -0.0012 0.0486  0.0548  330 LYS A C   
2635 O O   . LYS A 329 ? 0.5433 0.3986 0.3749 -0.0058 0.0608  0.0608  330 LYS A O   
2636 C CB  . LYS A 329 ? 0.5591 0.4035 0.3740 0.0106  0.0289  0.0618  330 LYS A CB  
2637 C CG  . LYS A 329 ? 0.6844 0.5198 0.4706 0.0113  0.0362  0.0688  330 LYS A CG  
2638 C CD  . LYS A 329 ? 0.6607 0.4743 0.4314 0.0111  0.0393  0.0822  330 LYS A CD  
2639 C CE  . LYS A 329 ? 0.7474 0.5522 0.4865 0.0126  0.0484  0.0902  330 LYS A CE  
2640 N NZ  . LYS A 329 ? 0.7989 0.5802 0.5212 0.0121  0.0527  0.1056  330 LYS A NZ  
2641 N N   . GLU A 330 ? 0.4939 0.3691 0.3396 0.0006  0.0445  0.0451  331 GLU A N   
2642 C CA  . GLU A 330 ? 0.5092 0.3936 0.3523 -0.0015 0.0517  0.0397  331 GLU A CA  
2643 C C   . GLU A 330 ? 0.4596 0.3540 0.3277 -0.0063 0.0569  0.0326  331 GLU A C   
2644 O O   . GLU A 330 ? 0.4530 0.3555 0.3219 -0.0076 0.0620  0.0265  331 GLU A O   
2645 C CB  . GLU A 330 ? 0.5245 0.4163 0.3585 0.0039  0.0423  0.0332  331 GLU A CB  
2646 C CG  . GLU A 330 ? 0.5650 0.4480 0.3738 0.0102  0.0357  0.0380  331 GLU A CG  
2647 C CD  . GLU A 330 ? 0.6890 0.5640 0.4726 0.0111  0.0446  0.0435  331 GLU A CD  
2648 O OE1 . GLU A 330 ? 0.7904 0.6708 0.5617 0.0146  0.0438  0.0376  331 GLU A OE1 
2649 O OE2 . GLU A 330 ? 0.7184 0.5815 0.4944 0.0086  0.0526  0.0537  331 GLU A OE2 
2650 N N   . ASN A 331 ? 0.3979 0.2912 0.2859 -0.0077 0.0545  0.0322  332 ASN A N   
2651 C CA  . ASN A 331 ? 0.3861 0.2877 0.2982 -0.0105 0.0574  0.0246  332 ASN A CA  
2652 C C   . ASN A 331 ? 0.3666 0.2795 0.2820 -0.0083 0.0540  0.0157  332 ASN A C   
2653 O O   . ASN A 331 ? 0.3828 0.3024 0.3077 -0.0106 0.0596  0.0094  332 ASN A O   
2654 C CB  . ASN A 331 ? 0.4517 0.3526 0.3715 -0.0171 0.0707  0.0261  332 ASN A CB  
2655 C CG  . ASN A 331 ? 0.5726 0.4642 0.5053 -0.0206 0.0726  0.0317  332 ASN A CG  
2656 O OD1 . ASN A 331 ? 0.5917 0.4727 0.5138 -0.0240 0.0795  0.0417  332 ASN A OD1 
2657 N ND2 . ASN A 331 ? 0.5907 0.4849 0.5460 -0.0190 0.0657  0.0253  332 ASN A ND2 
2658 N N   . ILE A 332 ? 0.3434 0.2585 0.2522 -0.0037 0.0445  0.0151  333 ILE A N   
2659 C CA  . ILE A 332 ? 0.3330 0.2566 0.2442 -0.0024 0.0410  0.0083  333 ILE A CA  
2660 C C   . ILE A 332 ? 0.3270 0.2546 0.2447 0.0015  0.0317  0.0079  333 ILE A C   
2661 O O   . ILE A 332 ? 0.3212 0.2462 0.2355 0.0045  0.0267  0.0123  333 ILE A O   
2662 C CB  . ILE A 332 ? 0.3627 0.2863 0.2557 -0.0018 0.0413  0.0078  333 ILE A CB  
2663 C CG1 . ILE A 332 ? 0.3854 0.3164 0.2845 -0.0018 0.0393  -0.0006 333 ILE A CG1 
2664 C CG2 . ILE A 332 ? 0.3841 0.3047 0.2643 0.0020  0.0332  0.0119  333 ILE A CG2 
2665 C CD1 . ILE A 332 ? 0.3987 0.3301 0.2817 -0.0004 0.0396  -0.0039 333 ILE A CD1 
2666 N N   . GLY A 333 ? 0.3132 0.2472 0.2402 0.0020  0.0297  0.0026  334 GLY A N   
2667 C CA  . GLY A 333 ? 0.3067 0.2458 0.2395 0.0053  0.0230  0.0033  334 GLY A CA  
2668 C C   . GLY A 333 ? 0.2920 0.2352 0.2302 0.0042  0.0219  -0.0010 334 GLY A C   
2669 O O   . GLY A 333 ? 0.2939 0.2361 0.2335 0.0020  0.0253  -0.0059 334 GLY A O   
2670 N N   . LEU A 334 ? 0.2862 0.2344 0.2288 0.0060  0.0173  0.0011  335 LEU A N   
2671 C CA  . LEU A 334 ? 0.2836 0.2340 0.2325 0.0042  0.0157  -0.0011 335 LEU A CA  
2672 C C   . LEU A 334 ? 0.2765 0.2314 0.2335 0.0071  0.0144  0.0027  335 LEU A C   
2673 O O   . LEU A 334 ? 0.2742 0.2341 0.2310 0.0102  0.0130  0.0068  335 LEU A O   
2674 C CB  . LEU A 334 ? 0.2899 0.2421 0.2354 0.0017  0.0118  -0.0021 335 LEU A CB  
2675 C CG  . LEU A 334 ? 0.2900 0.2430 0.2443 -0.0012 0.0089  -0.0048 335 LEU A CG  
2676 C CD1 . LEU A 334 ? 0.3062 0.2579 0.2549 -0.0028 0.0050  -0.0104 335 LEU A CD1 
2677 C CD2 . LEU A 334 ? 0.3020 0.2615 0.2667 -0.0016 0.0066  0.0006  335 LEU A CD2 
2678 N N   . VAL A 335 ? 0.2752 0.2282 0.2382 0.0067  0.0148  0.0015  336 VAL A N   
2679 C CA  . VAL A 335 ? 0.3108 0.2669 0.2788 0.0098  0.0148  0.0065  336 VAL A CA  
2680 C C   . VAL A 335 ? 0.2863 0.2405 0.2607 0.0053  0.0138  0.0078  336 VAL A C   
2681 O O   . VAL A 335 ? 0.2886 0.2360 0.2638 0.0028  0.0126  0.0024  336 VAL A O   
2682 C CB  . VAL A 335 ? 0.3094 0.2618 0.2771 0.0159  0.0159  0.0047  336 VAL A CB  
2683 C CG1 . VAL A 335 ? 0.3038 0.2577 0.2728 0.0201  0.0164  0.0107  336 VAL A CG1 
2684 C CG2 . VAL A 335 ? 0.2921 0.2459 0.2573 0.0204  0.0158  0.0031  336 VAL A CG2 
2685 N N   . MET A 336 ? 0.2788 0.2393 0.2592 0.0043  0.0141  0.0146  337 MET A N   
2686 C CA  . MET A 336 ? 0.2871 0.2449 0.2768 -0.0006 0.0137  0.0178  337 MET A CA  
2687 C C   . MET A 336 ? 0.3009 0.2606 0.2917 0.0031  0.0180  0.0268  337 MET A C   
2688 O O   . MET A 336 ? 0.2866 0.2568 0.2767 0.0067  0.0208  0.0319  337 MET A O   
2689 C CB  . MET A 336 ? 0.2845 0.2492 0.2842 -0.0068 0.0108  0.0182  337 MET A CB  
2690 C CG  . MET A 336 ? 0.3370 0.2978 0.3508 -0.0133 0.0095  0.0209  337 MET A CG  
2691 S SD  . MET A 336 ? 0.4082 0.3821 0.4405 -0.0197 0.0076  0.0238  337 MET A SD  
2692 C CE  . MET A 336 ? 0.4765 0.4568 0.5173 -0.0200 0.0165  0.0379  337 MET A CE  
2693 N N   . LEU A 337 ? 0.2936 0.2432 0.2851 0.0031  0.0184  0.0288  338 LEU A N   
2694 C CA  . LEU A 337 ? 0.3016 0.2503 0.2913 0.0070  0.0230  0.0389  338 LEU A CA  
2695 C C   . LEU A 337 ? 0.3355 0.2764 0.3359 -0.0005 0.0231  0.0444  338 LEU A C   
2696 O O   . LEU A 337 ? 0.3205 0.2503 0.3239 -0.0040 0.0180  0.0379  338 LEU A O   
2697 C CB  . LEU A 337 ? 0.3279 0.2682 0.3052 0.0168  0.0224  0.0363  338 LEU A CB  
2698 C CG  . LEU A 337 ? 0.3379 0.2821 0.3081 0.0235  0.0205  0.0281  338 LEU A CG  
2699 C CD1 . LEU A 337 ? 0.3304 0.2653 0.2931 0.0323  0.0180  0.0230  338 LEU A CD1 
2700 C CD2 . LEU A 337 ? 0.3132 0.2703 0.2807 0.0284  0.0232  0.0327  338 LEU A CD2 
2701 N N   . THR A 338 ? 0.3414 0.2884 0.3489 -0.0031 0.0290  0.0562  339 THR A N   
2702 C CA  . THR A 338 ? 0.3337 0.2712 0.3527 -0.0105 0.0301  0.0638  339 THR A CA  
2703 C C   . THR A 338 ? 0.3733 0.3113 0.3867 -0.0064 0.0392  0.0788  339 THR A C   
2704 O O   . THR A 338 ? 0.3671 0.3165 0.3701 0.0019  0.0444  0.0824  339 THR A O   
2705 C CB  . THR A 338 ? 0.4021 0.3470 0.4431 -0.0219 0.0283  0.0634  339 THR A CB  
2706 O OG1 . THR A 338 ? 0.4372 0.4015 0.4848 -0.0223 0.0345  0.0694  339 THR A OG1 
2707 C CG2 . THR A 338 ? 0.3752 0.3194 0.4185 -0.0243 0.0190  0.0486  339 THR A CG2 
2708 N N   . ASN A 339 ? 0.3645 0.2892 0.3840 -0.0114 0.0410  0.0879  340 ASN A N   
2709 C CA  . ASN A 339 ? 0.4204 0.3442 0.4344 -0.0086 0.0512  0.1048  340 ASN A CA  
2710 C C   . ASN A 339 ? 0.4570 0.3900 0.4946 -0.0209 0.0586  0.1163  340 ASN A C   
2711 O O   . ASN A 339 ? 0.4459 0.3722 0.4849 -0.0232 0.0669  0.1319  340 ASN A O   
2712 C CB  . ASN A 339 ? 0.4421 0.3419 0.4424 -0.0035 0.0491  0.1094  340 ASN A CB  
2713 C CG  . ASN A 339 ? 0.4174 0.2994 0.4320 -0.0131 0.0409  0.1051  340 ASN A CG  
2714 O OD1 . ASN A 339 ? 0.4123 0.3000 0.4476 -0.0237 0.0369  0.0989  340 ASN A OD1 
2715 N ND2 . ASN A 339 ? 0.4532 0.3129 0.4565 -0.0083 0.0373  0.1076  340 ASN A ND2 
2716 N N   . LYS A 340 ? 0.4210 0.3690 0.4777 -0.0286 0.0556  0.1088  341 LYS A N   
2717 C CA  . LYS A 340 ? 0.4453 0.4078 0.5279 -0.0393 0.0623  0.1172  341 LYS A CA  
2718 C C   . LYS A 340 ? 0.4120 0.3955 0.5045 -0.0402 0.0584  0.1060  341 LYS A C   
2719 O O   . LYS A 340 ? 0.4282 0.4088 0.5143 -0.0376 0.0482  0.0915  341 LYS A O   
2720 C CB  . LYS A 340 ? 0.4107 0.3592 0.5173 -0.0527 0.0583  0.1194  341 LYS A CB  
2721 C CG  . LYS A 340 ? 0.4118 0.3756 0.5500 -0.0649 0.0658  0.1287  341 LYS A CG  
2722 C CD  . LYS A 340 ? 0.4144 0.3632 0.5796 -0.0783 0.0591  0.1283  341 LYS A CD  
2723 C CE  . LYS A 340 ? 0.5152 0.4789 0.7163 -0.0915 0.0673  0.1384  341 LYS A CE  
2724 N NZ  . LYS A 340 ? 0.4840 0.4307 0.7139 -0.1046 0.0592  0.1373  341 LYS A NZ  
2725 N N   . ARG A 341 ? 0.4657 0.4705 0.5735 -0.0434 0.0670  0.1131  342 ARG A N   
2726 C CA  . ARG A 341 ? 0.4749 0.5004 0.5932 -0.0434 0.0629  0.1030  342 ARG A CA  
2727 C C   . ARG A 341 ? 0.4012 0.4222 0.5380 -0.0520 0.0503  0.0901  342 ARG A C   
2728 O O   . ARG A 341 ? 0.3515 0.3623 0.5073 -0.0621 0.0478  0.0920  342 ARG A O   
2729 C CB  . ARG A 341 ? 0.5349 0.5846 0.6722 -0.0466 0.0746  0.1130  342 ARG A CB  
2730 C CG  . ARG A 341 ? 0.6368 0.7076 0.7637 -0.0359 0.0766  0.1088  342 ARG A CG  
2731 C CD  . ARG A 341 ? 0.6704 0.7685 0.8252 -0.0413 0.0838  0.1124  342 ARG A CD  
2732 N NE  . ARG A 341 ? 0.6276 0.7291 0.8116 -0.0525 0.0744  0.1029  342 ARG A NE  
2733 C CZ  . ARG A 341 ? 0.5726 0.6763 0.7557 -0.0498 0.0610  0.0871  342 ARG A CZ  
2734 N NH1 . ARG A 341 ? 0.5640 0.6657 0.7202 -0.0379 0.0559  0.0798  342 ARG A NH1 
2735 N NH2 . ARG A 341 ? 0.5368 0.6439 0.7468 -0.0589 0.0521  0.0785  342 ARG A NH2 
2736 N N   . ILE A 342 ? 0.4182 0.4462 0.5484 -0.0472 0.0417  0.0768  343 ILE A N   
2737 C CA  . ILE A 342 ? 0.4041 0.4313 0.5474 -0.0521 0.0292  0.0632  343 ILE A CA  
2738 C C   . ILE A 342 ? 0.3849 0.4333 0.5319 -0.0480 0.0273  0.0573  343 ILE A C   
2739 O O   . ILE A 342 ? 0.3868 0.4410 0.5141 -0.0385 0.0307  0.0582  343 ILE A O   
2740 C CB  . ILE A 342 ? 0.4064 0.4150 0.5287 -0.0476 0.0198  0.0525  343 ILE A CB  
2741 C CG1 . ILE A 342 ? 0.4661 0.4539 0.5873 -0.0512 0.0195  0.0561  343 ILE A CG1 
2742 C CG2 . ILE A 342 ? 0.4376 0.4475 0.5661 -0.0490 0.0073  0.0379  343 ILE A CG2 
2743 C CD1 . ILE A 342 ? 0.4108 0.3830 0.5129 -0.0462 0.0111  0.0446  343 ILE A CD1 
2744 N N   . PRO A 343 ? 0.3480 0.4078 0.5198 -0.0538 0.0209  0.0504  344 PRO A N   
2745 C CA  . PRO A 343 ? 0.3896 0.4689 0.5638 -0.0484 0.0177  0.0439  344 PRO A CA  
2746 C C   . PRO A 343 ? 0.3969 0.4688 0.5401 -0.0376 0.0112  0.0358  344 PRO A C   
2747 O O   . PRO A 343 ? 0.3736 0.4290 0.5031 -0.0367 0.0033  0.0283  344 PRO A O   
2748 C CB  . PRO A 343 ? 0.3978 0.4838 0.6015 -0.0558 0.0075  0.0341  344 PRO A CB  
2749 C CG  . PRO A 343 ? 0.3791 0.4568 0.6059 -0.0676 0.0109  0.0409  344 PRO A CG  
2750 C CD  . PRO A 343 ? 0.3468 0.4021 0.5473 -0.0651 0.0150  0.0473  344 PRO A CD  
2751 N N   . ASN A 344 ? 0.4016 0.4857 0.5339 -0.0291 0.0150  0.0377  345 ASN A N   
2752 C CA  . ASN A 344 ? 0.4104 0.4873 0.5157 -0.0194 0.0092  0.0313  345 ASN A CA  
2753 C C   . ASN A 344 ? 0.3787 0.4490 0.4813 -0.0194 -0.0038 0.0191  345 ASN A C   
2754 O O   . ASN A 344 ? 0.3633 0.4182 0.4436 -0.0156 -0.0080 0.0148  345 ASN A O   
2755 C CB  . ASN A 344 ? 0.4292 0.5226 0.5303 -0.0107 0.0122  0.0327  345 ASN A CB  
2756 C CG  . ASN A 344 ? 0.5317 0.6259 0.6209 -0.0053 0.0229  0.0423  345 ASN A CG  
2757 O OD1 . ASN A 344 ? 0.5242 0.6018 0.5959 -0.0034 0.0245  0.0445  345 ASN A OD1 
2758 N ND2 . ASN A 344 ? 0.5510 0.6656 0.6495 -0.0016 0.0299  0.0472  345 ASN A ND2 
2759 N N   . GLU A 345 ? 0.3357 0.4183 0.4612 -0.0231 -0.0100 0.0133  346 GLU A N   
2760 C CA  . GLU A 345 ? 0.3587 0.4355 0.4820 -0.0218 -0.0236 0.0009  346 GLU A CA  
2761 C C   . GLU A 345 ? 0.3864 0.4425 0.4971 -0.0243 -0.0269 -0.0024 346 GLU A C   
2762 O O   . GLU A 345 ? 0.3602 0.4054 0.4491 -0.0186 -0.0339 -0.0094 346 GLU A O   
2763 C CB  . GLU A 345 ? 0.4142 0.5070 0.5714 -0.0273 -0.0298 -0.0051 346 GLU A CB  
2764 C CG  . GLU A 345 ? 0.4280 0.5127 0.5905 -0.0285 -0.0441 -0.0181 346 GLU A CG  
2765 C CD  . GLU A 345 ? 0.5302 0.6059 0.7109 -0.0386 -0.0438 -0.0173 346 GLU A CD  
2766 O OE1 . GLU A 345 ? 0.5751 0.6609 0.7862 -0.0478 -0.0373 -0.0108 346 GLU A OE1 
2767 O OE2 . GLU A 345 ? 0.5495 0.6077 0.7141 -0.0371 -0.0498 -0.0230 346 GLU A OE2 
2768 N N   . GLU A 346 ? 0.3573 0.4075 0.4806 -0.0322 -0.0217 0.0030  347 GLU A N   
2769 C CA  . GLU A 346 ? 0.3617 0.3934 0.4757 -0.0341 -0.0258 -0.0015 347 GLU A CA  
2770 C C   . GLU A 346 ? 0.3388 0.3577 0.4223 -0.0280 -0.0210 0.0010  347 GLU A C   
2771 O O   . GLU A 346 ? 0.3345 0.3412 0.4029 -0.0257 -0.0261 -0.0062 347 GLU A O   
2772 C CB  . GLU A 346 ? 0.4191 0.4463 0.5554 -0.0437 -0.0221 0.0041  347 GLU A CB  
2773 C CG  . GLU A 346 ? 0.4357 0.4735 0.6074 -0.0516 -0.0278 0.0005  347 GLU A CG  
2774 C CD  . GLU A 346 ? 0.4771 0.5056 0.6556 -0.0527 -0.0424 -0.0137 347 GLU A CD  
2775 O OE1 . GLU A 346 ? 0.4380 0.4677 0.6476 -0.0611 -0.0471 -0.0160 347 GLU A OE1 
2776 O OE2 . GLU A 346 ? 0.4773 0.4973 0.6303 -0.0447 -0.0492 -0.0226 347 GLU A OE2 
2777 N N   . ARG A 347 ? 0.3271 0.3494 0.4024 -0.0251 -0.0114 0.0103  348 ARG A N   
2778 C CA  . ARG A 347 ? 0.3546 0.3657 0.4049 -0.0195 -0.0076 0.0116  348 ARG A CA  
2779 C C   . ARG A 347 ? 0.3340 0.3430 0.3656 -0.0131 -0.0130 0.0050  348 ARG A C   
2780 O O   . ARG A 347 ? 0.3439 0.3410 0.3584 -0.0109 -0.0138 0.0014  348 ARG A O   
2781 C CB  . ARG A 347 ? 0.3444 0.3607 0.3909 -0.0160 0.0019  0.0213  348 ARG A CB  
2782 C CG  . ARG A 347 ? 0.3886 0.4093 0.4517 -0.0211 0.0092  0.0307  348 ARG A CG  
2783 C CD  . ARG A 347 ? 0.3990 0.4264 0.4539 -0.0146 0.0181  0.0394  348 ARG A CD  
2784 N NE  . ARG A 347 ? 0.4606 0.4992 0.5324 -0.0184 0.0260  0.0494  348 ARG A NE  
2785 C CZ  . ARG A 347 ? 0.5031 0.5515 0.5705 -0.0125 0.0346  0.0576  348 ARG A CZ  
2786 N NH1 . ARG A 347 ? 0.4369 0.4845 0.4847 -0.0022 0.0349  0.0562  348 ARG A NH1 
2787 N NH2 . ARG A 347 ? 0.5194 0.5791 0.6033 -0.0170 0.0432  0.0675  348 ARG A NH2 
2788 N N   . ILE A 348 ? 0.3639 0.3844 0.3987 -0.0098 -0.0165 0.0039  349 ILE A N   
2789 C CA  . ILE A 348 ? 0.3521 0.3690 0.3678 -0.0030 -0.0220 -0.0007 349 ILE A CA  
2790 C C   . ILE A 348 ? 0.3508 0.3590 0.3591 -0.0030 -0.0303 -0.0096 349 ILE A C   
2791 O O   . ILE A 348 ? 0.3745 0.3716 0.3606 0.0009  -0.0306 -0.0115 349 ILE A O   
2792 C CB  . ILE A 348 ? 0.3547 0.3860 0.3773 0.0014  -0.0254 -0.0008 349 ILE A CB  
2793 C CG1 . ILE A 348 ? 0.3138 0.3537 0.3397 0.0037  -0.0170 0.0073  349 ILE A CG1 
2794 C CG2 . ILE A 348 ? 0.3682 0.3929 0.3701 0.0089  -0.0327 -0.0052 349 ILE A CG2 
2795 C CD1 . ILE A 348 ? 0.3568 0.4147 0.3942 0.0080  -0.0195 0.0067  349 ILE A CD1 
2796 N N   . LYS A 349 ? 0.3470 0.3603 0.3742 -0.0071 -0.0368 -0.0153 350 LYS A N   
2797 C CA  . LYS A 349 ? 0.3730 0.3791 0.3933 -0.0052 -0.0464 -0.0256 350 LYS A CA  
2798 C C   . LYS A 349 ? 0.3939 0.3862 0.4003 -0.0061 -0.0429 -0.0269 350 LYS A C   
2799 O O   . LYS A 349 ? 0.3620 0.3460 0.3469 -0.0009 -0.0459 -0.0321 350 LYS A O   
2800 C CB  . LYS A 349 ? 0.3688 0.3831 0.4171 -0.0099 -0.0550 -0.0325 350 LYS A CB  
2801 C CG  . LYS A 349 ? 0.4231 0.4515 0.4837 -0.0068 -0.0627 -0.0367 350 LYS A CG  
2802 C CD  . LYS A 349 ? 0.4251 0.4618 0.5183 -0.0124 -0.0716 -0.0449 350 LYS A CD  
2803 C CE  . LYS A 349 ? 0.4281 0.4824 0.5399 -0.0101 -0.0786 -0.0495 350 LYS A CE  
2804 N NZ  . LYS A 349 ? 0.5364 0.6007 0.6868 -0.0174 -0.0859 -0.0567 350 LYS A NZ  
2805 N N   . ALA A 350 ? 0.3659 0.3557 0.3839 -0.0121 -0.0364 -0.0221 351 ALA A N   
2806 C CA  . ALA A 350 ? 0.3662 0.3439 0.3736 -0.0125 -0.0339 -0.0247 351 ALA A CA  
2807 C C   . ALA A 350 ? 0.3710 0.3428 0.3540 -0.0077 -0.0269 -0.0217 351 ALA A C   
2808 O O   . ALA A 350 ? 0.3645 0.3289 0.3320 -0.0049 -0.0270 -0.0270 351 ALA A O   
2809 C CB  . ALA A 350 ? 0.3279 0.3030 0.3521 -0.0188 -0.0291 -0.0195 351 ALA A CB  
2810 N N   . ALA A 351 ? 0.3641 0.3396 0.3445 -0.0065 -0.0205 -0.0134 352 ALA A N   
2811 C CA  . ALA A 351 ? 0.3385 0.3081 0.2998 -0.0027 -0.0146 -0.0107 352 ALA A CA  
2812 C C   . ALA A 351 ? 0.3440 0.3105 0.2865 0.0023  -0.0184 -0.0137 352 ALA A C   
2813 O O   . ALA A 351 ? 0.3472 0.3060 0.2729 0.0043  -0.0142 -0.0141 352 ALA A O   
2814 C CB  . ALA A 351 ? 0.2987 0.2726 0.2628 -0.0014 -0.0092 -0.0028 352 ALA A CB  
2815 N N   . TYR A 352 ? 0.3256 0.2979 0.2705 0.0048  -0.0261 -0.0156 353 TYR A N   
2816 C CA  . TYR A 352 ? 0.3552 0.3228 0.2797 0.0111  -0.0312 -0.0184 353 TYR A CA  
2817 C C   . TYR A 352 ? 0.3657 0.3265 0.2772 0.0128  -0.0334 -0.0257 353 TYR A C   
2818 O O   . TYR A 352 ? 0.3686 0.3214 0.2567 0.0172  -0.0305 -0.0248 353 TYR A O   
2819 C CB  . TYR A 352 ? 0.3499 0.3262 0.2826 0.0142  -0.0412 -0.0215 353 TYR A CB  
2820 C CG  . TYR A 352 ? 0.3631 0.3333 0.2728 0.0226  -0.0484 -0.0244 353 TYR A CG  
2821 C CD1 . TYR A 352 ? 0.3796 0.3468 0.2802 0.0268  -0.0570 -0.0335 353 TYR A CD1 
2822 C CD2 . TYR A 352 ? 0.4060 0.3725 0.3023 0.0273  -0.0476 -0.0183 353 TYR A CD2 
2823 C CE1 . TYR A 352 ? 0.4358 0.3961 0.3116 0.0362  -0.0639 -0.0356 353 TYR A CE1 
2824 C CE2 . TYR A 352 ? 0.4140 0.3724 0.2869 0.0356  -0.0544 -0.0197 353 TYR A CE2 
2825 C CZ  . TYR A 352 ? 0.4397 0.3951 0.3014 0.0403  -0.0622 -0.0279 353 TYR A CZ  
2826 O OH  . TYR A 352 ? 0.4293 0.3753 0.2641 0.0502  -0.0691 -0.0286 353 TYR A OH  
2827 N N   . ALA A 353 ? 0.3598 0.3234 0.2865 0.0098  -0.0383 -0.0328 354 ALA A N   
2828 C CA  . ALA A 353 ? 0.3829 0.3410 0.2976 0.0132  -0.0422 -0.0419 354 ALA A CA  
2829 C C   . ALA A 353 ? 0.4115 0.3634 0.3143 0.0124  -0.0317 -0.0401 354 ALA A C   
2830 O O   . ALA A 353 ? 0.4183 0.3654 0.2995 0.0176  -0.0300 -0.0435 354 ALA A O   
2831 C CB  . ALA A 353 ? 0.3690 0.3308 0.3061 0.0102  -0.0516 -0.0510 354 ALA A CB  
2832 N N   . VAL A 354 ? 0.3640 0.3163 0.2801 0.0066  -0.0242 -0.0349 355 VAL A N   
2833 C CA  . VAL A 354 ? 0.3575 0.3054 0.2662 0.0059  -0.0147 -0.0344 355 VAL A CA  
2834 C C   . VAL A 354 ? 0.4265 0.3709 0.3156 0.0085  -0.0068 -0.0279 355 VAL A C   
2835 O O   . VAL A 354 ? 0.4436 0.3848 0.3171 0.0109  -0.0012 -0.0299 355 VAL A O   
2836 C CB  . VAL A 354 ? 0.3785 0.3271 0.3055 0.0006  -0.0103 -0.0307 355 VAL A CB  
2837 C CG1 . VAL A 354 ? 0.4192 0.3645 0.3402 0.0006  -0.0009 -0.0305 355 VAL A CG1 
2838 C CG2 . VAL A 354 ? 0.3769 0.3257 0.3218 -0.0024 -0.0172 -0.0362 355 VAL A CG2 
2839 N N   . LEU A 355 ? 0.3775 0.3226 0.2679 0.0082  -0.0059 -0.0200 356 LEU A N   
2840 C CA  . LEU A 355 ? 0.4037 0.3433 0.2787 0.0097  0.0013  -0.0131 356 LEU A CA  
2841 C C   . LEU A 355 ? 0.4306 0.3648 0.2810 0.0154  -0.0005 -0.0135 356 LEU A C   
2842 O O   . LEU A 355 ? 0.4701 0.3983 0.3048 0.0162  0.0080  -0.0090 356 LEU A O   
2843 C CB  . LEU A 355 ? 0.4248 0.3657 0.3072 0.0094  0.0006  -0.0059 356 LEU A CB  
2844 C CG  . LEU A 355 ? 0.4527 0.3975 0.3540 0.0057  0.0044  -0.0042 356 LEU A CG  
2845 C CD1 . LEU A 355 ? 0.4767 0.4239 0.3829 0.0076  0.0028  0.0016  356 LEU A CD1 
2846 C CD2 . LEU A 355 ? 0.4273 0.3681 0.3280 0.0036  0.0134  -0.0045 356 LEU A CD2 
2847 N N   . ASN A 356 ? 0.4008 0.3369 0.2476 0.0198  -0.0114 -0.0186 357 ASN A N   
2848 C CA  . ASN A 356 ? 0.4176 0.3478 0.2380 0.0273  -0.0146 -0.0197 357 ASN A CA  
2849 C C   . ASN A 356 ? 0.4761 0.4049 0.2825 0.0301  -0.0108 -0.0260 357 ASN A C   
2850 O O   . ASN A 356 ? 0.5159 0.4387 0.2952 0.0370  -0.0095 -0.0250 357 ASN A O   
2851 C CB  . ASN A 356 ? 0.4208 0.3545 0.2435 0.0325  -0.0293 -0.0257 357 ASN A CB  
2852 C CG  . ASN A 356 ? 0.4418 0.3740 0.2627 0.0347  -0.0330 -0.0190 357 ASN A CG  
2853 O OD1 . ASN A 356 ? 0.5033 0.4278 0.3010 0.0422  -0.0370 -0.0170 357 ASN A OD1 
2854 N ND2 . ASN A 356 ? 0.4337 0.3727 0.2774 0.0294  -0.0320 -0.0156 357 ASN A ND2 
2855 N N   . ALA A 357 ? 0.4554 0.3893 0.2779 0.0261  -0.0090 -0.0326 358 ALA A N   
2856 C CA  . ALA A 357 ? 0.5058 0.4400 0.3162 0.0300  -0.0065 -0.0406 358 ALA A CA  
2857 C C   . ALA A 357 ? 0.5962 0.5306 0.4046 0.0264  0.0086  -0.0369 358 ALA A C   
2858 O O   . ALA A 357 ? 0.5959 0.5315 0.3899 0.0306  0.0136  -0.0419 358 ALA A O   
2859 C CB  . ALA A 357 ? 0.4774 0.4165 0.3067 0.0295  -0.0167 -0.0529 358 ALA A CB  
2860 N N   . ILE A 358 ? 0.5497 0.4840 0.3731 0.0193  0.0157  -0.0293 359 ILE A N   
2861 C CA  . ILE A 358 ? 0.6025 0.5385 0.4301 0.0156  0.0287  -0.0280 359 ILE A CA  
2862 C C   . ILE A 358 ? 0.7163 0.6482 0.5207 0.0177  0.0399  -0.0206 359 ILE A C   
2863 O O   . ILE A 358 ? 0.7553 0.6801 0.5496 0.0178  0.0408  -0.0107 359 ILE A O   
2864 C CB  . ILE A 358 ? 0.5623 0.4991 0.4124 0.0090  0.0315  -0.0231 359 ILE A CB  
2865 C CG1 . ILE A 358 ? 0.5759 0.5163 0.4466 0.0072  0.0232  -0.0300 359 ILE A CG1 
2866 C CG2 . ILE A 358 ? 0.6362 0.5744 0.4905 0.0055  0.0446  -0.0213 359 ILE A CG2 
2867 C CD1 . ILE A 358 ? 0.5011 0.4426 0.3910 0.0028  0.0268  -0.0276 359 ILE A CD1 
2868 N N   . LYS A 359 ? 0.7841 0.7203 0.5796 0.0198  0.0485  -0.0253 360 LYS A N   
2869 C CA  . LYS A 359 ? 0.8496 0.7830 0.6242 0.0210  0.0623  -0.0172 360 LYS A CA  
2870 C C   . LYS A 359 ? 0.8952 0.8269 0.6853 0.0124  0.0735  -0.0076 360 LYS A C   
2871 O O   . LYS A 359 ? 0.8130 0.7499 0.6290 0.0070  0.0739  -0.0117 360 LYS A O   
2872 C CB  . LYS A 359 ? 0.8879 0.8296 0.6522 0.0255  0.0699  -0.0256 360 LYS A CB  
2873 C CG  . LYS A 359 ? 0.9306 0.8755 0.6867 0.0343  0.0567  -0.0393 360 LYS A CG  
2874 C CD  . LYS A 359 ? 1.0296 0.9832 0.7724 0.0406  0.0650  -0.0478 360 LYS A CD  
2875 C CE  . LYS A 359 ? 0.9949 0.9511 0.7298 0.0507  0.0502  -0.0632 360 LYS A CE  
2876 N NZ  . LYS A 359 ? 0.9563 0.9150 0.7212 0.0469  0.0384  -0.0741 360 LYS A NZ  
2877 N N   . LYS A 360 ? 1.0185 0.9419 0.7927 0.0116  0.0819  0.0049  361 LYS A N   
2878 C CA  . LYS A 360 ? 1.0307 0.9505 0.8204 0.0034  0.0915  0.0142  361 LYS A CA  
2879 C C   . LYS A 360 ? 1.0157 0.9459 0.8226 -0.0019 0.1055  0.0102  361 LYS A C   
2880 O O   . LYS A 360 ? 0.9814 0.9104 0.8047 -0.0090 0.1144  0.0162  361 LYS A O   
2881 C CB  . LYS A 360 ? 1.0249 0.9312 0.7920 0.0040  0.0976  0.0290  361 LYS A CB  
2882 C CG  . LYS A 360 ? 1.0520 0.9496 0.7901 0.0132  0.0863  0.0309  361 LYS A CG  
2883 C CD  . LYS A 360 ? 0.9743 0.8687 0.7236 0.0143  0.0697  0.0289  361 LYS A CD  
2884 C CE  . LYS A 360 ? 0.9308 0.8174 0.6534 0.0239  0.0580  0.0298  361 LYS A CE  
2885 N NZ  . LYS A 360 ? 0.8730 0.7450 0.5661 0.0273  0.0650  0.0431  361 LYS A NZ  
2886 O OXT . LYS A 360 ? 0.9876 0.9284 0.7943 0.0011  0.1076  -0.0001 361 LYS A OXT 
2887 N N   . ASN B 2   ? 1.0392 0.8423 0.9986 -0.0706 -0.0605 -0.1486 3   ASN B N   
2888 C CA  . ASN B 2   ? 1.0135 0.8389 0.9741 -0.0638 -0.0632 -0.1389 3   ASN B CA  
2889 C C   . ASN B 2   ? 0.9996 0.8299 0.9392 -0.0623 -0.0736 -0.1463 3   ASN B C   
2890 O O   . ASN B 2   ? 1.0169 0.8323 0.9312 -0.0556 -0.0703 -0.1516 3   ASN B O   
2891 C CB  . ASN B 2   ? 1.0228 0.8457 0.9800 -0.0517 -0.0503 -0.1283 3   ASN B CB  
2892 C CG  . ASN B 2   ? 1.0931 0.9204 1.0737 -0.0520 -0.0431 -0.1173 3   ASN B CG  
2893 O OD1 . ASN B 2   ? 1.0755 0.9202 1.0742 -0.0564 -0.0476 -0.1109 3   ASN B OD1 
2894 N ND2 . ASN B 2   ? 1.1532 0.9638 1.1328 -0.0471 -0.0318 -0.1151 3   ASN B ND2 
2895 N N   . THR B 3   ? 0.9693 0.8200 0.9194 -0.0679 -0.0859 -0.1461 4   THR B N   
2896 C CA  . THR B 3   ? 1.0172 0.8754 0.9503 -0.0674 -0.0986 -0.1527 4   THR B CA  
2897 C C   . THR B 3   ? 1.0297 0.8870 0.9393 -0.0544 -0.0935 -0.1480 4   THR B C   
2898 O O   . THR B 3   ? 0.9714 0.8296 0.8848 -0.0464 -0.0814 -0.1374 4   THR B O   
2899 C CB  . THR B 3   ? 0.9985 0.8831 0.9530 -0.0736 -0.1103 -0.1490 4   THR B CB  
2900 O OG1 . THR B 3   ? 0.9281 0.8290 0.8963 -0.0675 -0.1037 -0.1342 4   THR B OG1 
2901 C CG2 . THR B 3   ? 0.9708 0.8559 0.9494 -0.0869 -0.1146 -0.1541 4   THR B CG2 
2902 N N   . PRO B 4   ? 1.0785 0.9334 0.9633 -0.0517 -0.1023 -0.1555 5   PRO B N   
2903 C CA  . PRO B 4   ? 1.0618 0.9158 0.9239 -0.0391 -0.0966 -0.1503 5   PRO B CA  
2904 C C   . PRO B 4   ? 0.9931 0.8702 0.8698 -0.0339 -0.0945 -0.1360 5   PRO B C   
2905 O O   . PRO B 4   ? 0.9415 0.8173 0.8077 -0.0237 -0.0847 -0.1285 5   PRO B O   
2906 C CB  . PRO B 4   ? 1.1742 1.0234 1.0091 -0.0393 -0.1098 -0.1614 5   PRO B CB  
2907 C CG  . PRO B 4   ? 1.1414 0.9791 0.9789 -0.0509 -0.1183 -0.1749 5   PRO B CG  
2908 C CD  . PRO B 4   ? 1.0945 0.9443 0.9687 -0.0599 -0.1171 -0.1698 5   PRO B CD  
2909 N N   . LYS B 5   ? 0.9736 0.8713 0.8748 -0.0409 -0.1030 -0.1321 6   LYS B N   
2910 C CA  . LYS B 5   ? 0.9040 0.8227 0.8186 -0.0363 -0.1012 -0.1188 6   LYS B CA  
2911 C C   . LYS B 5   ? 0.8074 0.7247 0.7371 -0.0329 -0.0866 -0.1081 6   LYS B C   
2912 O O   . LYS B 5   ? 0.7500 0.6721 0.6759 -0.0242 -0.0790 -0.0987 6   LYS B O   
2913 C CB  . LYS B 5   ? 0.8693 0.8090 0.8065 -0.0446 -0.1134 -0.1178 6   LYS B CB  
2914 C CG  . LYS B 5   ? 0.7743 0.7353 0.7218 -0.0396 -0.1133 -0.1053 6   LYS B CG  
2915 C CD  . LYS B 5   ? 0.8057 0.7704 0.7288 -0.0310 -0.1180 -0.1049 6   LYS B CD  
2916 C CE  . LYS B 5   ? 0.7058 0.6928 0.6413 -0.0278 -0.1204 -0.0937 6   LYS B CE  
2917 N NZ  . LYS B 5   ? 0.8228 0.8131 0.7343 -0.0191 -0.1252 -0.0929 6   LYS B NZ  
2918 N N   . ASP B 6   ? 0.8195 0.7298 0.7665 -0.0397 -0.0830 -0.1094 7   ASP B N   
2919 C CA  . ASP B 6   ? 0.7723 0.6794 0.7325 -0.0364 -0.0702 -0.1000 7   ASP B CA  
2920 C C   . ASP B 6   ? 0.7619 0.6554 0.7039 -0.0261 -0.0590 -0.0984 7   ASP B C   
2921 O O   . ASP B 6   ? 0.6343 0.5337 0.5817 -0.0192 -0.0507 -0.0880 7   ASP B O   
2922 C CB  . ASP B 6   ? 0.7898 0.6861 0.7653 -0.0447 -0.0679 -0.1036 7   ASP B CB  
2923 C CG  . ASP B 6   ? 0.7839 0.6946 0.7828 -0.0544 -0.0755 -0.1022 7   ASP B CG  
2924 O OD1 . ASP B 6   ? 0.8704 0.7841 0.8692 -0.0619 -0.0864 -0.1112 7   ASP B OD1 
2925 O OD2 . ASP B 6   ? 0.7489 0.6675 0.7663 -0.0547 -0.0705 -0.0921 7   ASP B OD2 
2926 N N   . GLN B 7   ? 0.7729 0.6478 0.6935 -0.0249 -0.0584 -0.1090 8   GLN B N   
2927 C CA  . GLN B 7   ? 0.7433 0.6031 0.6478 -0.0152 -0.0461 -0.1081 8   GLN B CA  
2928 C C   . GLN B 7   ? 0.6935 0.5625 0.5857 -0.0059 -0.0434 -0.1014 8   GLN B C   
2929 O O   . GLN B 7   ? 0.6840 0.5511 0.5770 0.0021  -0.0316 -0.0940 8   GLN B O   
2930 C CB  . GLN B 7   ? 0.7853 0.6217 0.6674 -0.0162 -0.0461 -0.1215 8   GLN B CB  
2931 C CG  . GLN B 7   ? 0.8441 0.6674 0.7378 -0.0243 -0.0454 -0.1275 8   GLN B CG  
2932 C CD  . GLN B 7   ? 0.9312 0.7286 0.8016 -0.0245 -0.0435 -0.1405 8   GLN B CD  
2933 O OE1 . GLN B 7   ? 0.9306 0.7193 0.7745 -0.0185 -0.0432 -0.1455 8   GLN B OE1 
2934 N NE2 . GLN B 7   ? 0.9294 0.7127 0.8080 -0.0312 -0.0417 -0.1460 8   GLN B NE2 
2935 N N   . GLU B 8   ? 0.6830 0.5624 0.5649 -0.0067 -0.0540 -0.1036 9   GLU B N   
2936 C CA  . GLU B 8   ? 0.7124 0.5992 0.5815 0.0025  -0.0507 -0.0969 9   GLU B CA  
2937 C C   . GLU B 8   ? 0.5976 0.5031 0.4888 0.0042  -0.0469 -0.0833 9   GLU B C   
2938 O O   . GLU B 8   ? 0.5682 0.4754 0.4554 0.0123  -0.0375 -0.0756 9   GLU B O   
2939 C CB  . GLU B 8   ? 0.7391 0.6307 0.5892 0.0021  -0.0634 -0.1027 9   GLU B CB  
2940 C CG  . GLU B 8   ? 0.7900 0.6932 0.6311 0.0104  -0.0617 -0.0938 9   GLU B CG  
2941 C CD  . GLU B 8   ? 0.8713 0.7612 0.6924 0.0214  -0.0475 -0.0910 9   GLU B CD  
2942 O OE1 . GLU B 8   ? 0.9372 0.8268 0.7363 0.0279  -0.0485 -0.0903 9   GLU B OE1 
2943 O OE2 . GLU B 8   ? 0.7758 0.6559 0.6034 0.0238  -0.0350 -0.0889 9   GLU B OE2 
2944 N N   . ILE B 9   ? 0.6147 0.5336 0.5293 -0.0035 -0.0534 -0.0801 10  ILE B N   
2945 C CA  . ILE B 9   ? 0.5575 0.4925 0.4912 -0.0021 -0.0500 -0.0675 10  ILE B CA  
2946 C C   . ILE B 9   ? 0.5525 0.4810 0.4981 0.0010  -0.0379 -0.0614 10  ILE B C   
2947 O O   . ILE B 9   ? 0.4962 0.4321 0.4477 0.0064  -0.0312 -0.0517 10  ILE B O   
2948 C CB  . ILE B 9   ? 0.5379 0.4880 0.4918 -0.0107 -0.0598 -0.0659 10  ILE B CB  
2949 C CG1 . ILE B 9   ? 0.5465 0.5057 0.4903 -0.0126 -0.0724 -0.0710 10  ILE B CG1 
2950 C CG2 . ILE B 9   ? 0.4958 0.4599 0.4683 -0.0094 -0.0556 -0.0531 10  ILE B CG2 
2951 C CD1 . ILE B 9   ? 0.6165 0.5932 0.5815 -0.0198 -0.0813 -0.0681 10  ILE B CD1 
2952 N N   . LYS B 10  ? 0.5266 0.4411 0.4762 -0.0024 -0.0351 -0.0669 11  LYS B N   
2953 C CA  . LYS B 10  ? 0.5344 0.4415 0.4938 0.0015  -0.0239 -0.0615 11  LYS B CA  
2954 C C   . LYS B 10  ? 0.5149 0.4155 0.4604 0.0116  -0.0138 -0.0595 11  LYS B C   
2955 O O   . LYS B 10  ? 0.4826 0.3866 0.4391 0.0166  -0.0055 -0.0510 11  LYS B O   
2956 C CB  . LYS B 10  ? 0.5874 0.4782 0.5503 -0.0032 -0.0226 -0.0686 11  LYS B CB  
2957 C CG  . LYS B 10  ? 0.6690 0.5443 0.6284 0.0039  -0.0105 -0.0681 11  LYS B CG  
2958 C CD  . LYS B 10  ? 0.6583 0.5218 0.6303 0.0002  -0.0074 -0.0694 11  LYS B CD  
2959 C CE  . LYS B 10  ? 0.6926 0.5468 0.6678 0.0088  0.0048  -0.0647 11  LYS B CE  
2960 N NZ  . LYS B 10  ? 0.7026 0.5465 0.6580 0.0166  0.0120  -0.0692 11  LYS B NZ  
2961 N N   . LYS B 11  ? 0.5153 0.4064 0.4369 0.0146  -0.0143 -0.0674 12  LYS B N   
2962 C CA  . LYS B 11  ? 0.5348 0.4186 0.4415 0.0244  -0.0034 -0.0657 12  LYS B CA  
2963 C C   . LYS B 11  ? 0.5190 0.4184 0.4285 0.0292  -0.0013 -0.0557 12  LYS B C   
2964 O O   . LYS B 11  ? 0.4575 0.3563 0.3697 0.0362  0.0098  -0.0494 12  LYS B O   
2965 C CB  . LYS B 11  ? 0.5781 0.4463 0.4553 0.0264  -0.0050 -0.0766 12  LYS B CB  
2966 C CG  . LYS B 11  ? 0.6444 0.5008 0.5043 0.0368  0.0082  -0.0758 12  LYS B CG  
2967 C CD  . LYS B 11  ? 0.7081 0.5407 0.5443 0.0380  0.0106  -0.0878 12  LYS B CD  
2968 C CE  . LYS B 11  ? 0.7728 0.5932 0.5844 0.0484  0.0221  -0.0882 12  LYS B CE  
2969 N NZ  . LYS B 11  ? 0.8544 0.6492 0.6403 0.0501  0.0253  -0.1000 12  LYS B NZ  
2970 N N   . LEU B 12  ? 0.4759 0.3891 0.3852 0.0257  -0.0114 -0.0541 13  LEU B N   
2971 C CA  . LEU B 12  ? 0.5057 0.4329 0.4174 0.0300  -0.0092 -0.0445 13  LEU B CA  
2972 C C   . LEU B 12  ? 0.4789 0.4159 0.4160 0.0295  -0.0042 -0.0342 13  LEU B C   
2973 O O   . LEU B 12  ? 0.4458 0.3872 0.3857 0.0352  0.0040  -0.0267 13  LEU B O   
2974 C CB  . LEU B 12  ? 0.5095 0.4492 0.4171 0.0263  -0.0214 -0.0448 13  LEU B CB  
2975 C CG  . LEU B 12  ? 0.5881 0.5206 0.4675 0.0292  -0.0265 -0.0526 13  LEU B CG  
2976 C CD1 . LEU B 12  ? 0.5525 0.4995 0.4319 0.0257  -0.0396 -0.0522 13  LEU B CD1 
2977 C CD2 . LEU B 12  ? 0.6174 0.5433 0.4790 0.0392  -0.0152 -0.0489 13  LEU B CD2 
2978 N N   . VAL B 13  ? 0.4788 0.4190 0.4340 0.0226  -0.0092 -0.0338 14  VAL B N   
2979 C CA  . VAL B 13  ? 0.3902 0.3380 0.3675 0.0221  -0.0057 -0.0245 14  VAL B CA  
2980 C C   . VAL B 13  ? 0.4264 0.3652 0.4083 0.0278  0.0054  -0.0225 14  VAL B C   
2981 O O   . VAL B 13  ? 0.4368 0.3825 0.4299 0.0315  0.0111  -0.0141 14  VAL B O   
2982 C CB  . VAL B 13  ? 0.4092 0.3598 0.4018 0.0138  -0.0130 -0.0249 14  VAL B CB  
2983 C CG1 . VAL B 13  ? 0.4345 0.3903 0.4470 0.0137  -0.0096 -0.0156 14  VAL B CG1 
2984 C CG2 . VAL B 13  ? 0.3912 0.3534 0.3827 0.0087  -0.0232 -0.0256 14  VAL B CG2 
2985 N N   . ASP B 14  ? 0.4153 0.3385 0.3895 0.0286  0.0086  -0.0303 15  ASP B N   
2986 C CA  . ASP B 14  ? 0.4681 0.3817 0.4455 0.0351  0.0198  -0.0291 15  ASP B CA  
2987 C C   . ASP B 14  ? 0.4627 0.3794 0.4331 0.0429  0.0287  -0.0248 15  ASP B C   
2988 O O   . ASP B 14  ? 0.4445 0.3651 0.4289 0.0474  0.0365  -0.0177 15  ASP B O   
2989 C CB  . ASP B 14  ? 0.5164 0.4109 0.4805 0.0354  0.0222  -0.0394 15  ASP B CB  
2990 C CG  . ASP B 14  ? 0.5259 0.4133 0.5034 0.0308  0.0204  -0.0410 15  ASP B CG  
2991 O OD1 . ASP B 14  ? 0.5043 0.3998 0.5016 0.0298  0.0200  -0.0332 15  ASP B OD1 
2992 O OD2 . ASP B 14  ? 0.5890 0.4613 0.5559 0.0284  0.0195  -0.0503 15  ASP B OD2 
2993 N N   . GLN B 15  ? 0.4665 0.3803 0.4147 0.0448  0.0278  -0.0293 16  GLN B N   
2994 C CA  . GLN B 15  ? 0.4621 0.3758 0.4001 0.0526  0.0374  -0.0257 16  GLN B CA  
2995 C C   . GLN B 15  ? 0.4495 0.3797 0.4040 0.0534  0.0392  -0.0148 16  GLN B C   
2996 O O   . GLN B 15  ? 0.4713 0.4025 0.4315 0.0593  0.0500  -0.0095 16  GLN B O   
2997 C CB  . GLN B 15  ? 0.4967 0.4054 0.4065 0.0540  0.0337  -0.0317 16  GLN B CB  
2998 C CG  . GLN B 15  ? 0.6178 0.5066 0.5043 0.0566  0.0365  -0.0422 16  GLN B CG  
2999 C CD  . GLN B 15  ? 0.7245 0.6092 0.5820 0.0583  0.0314  -0.0472 16  GLN B CD  
3000 O OE1 . GLN B 15  ? 0.7188 0.6080 0.5711 0.0523  0.0180  -0.0518 16  GLN B OE1 
3001 N NE2 . GLN B 15  ? 0.8006 0.6774 0.6401 0.0666  0.0421  -0.0460 16  GLN B NE2 
3002 N N   . ASN B 16  ? 0.4524 0.3950 0.4150 0.0475  0.0291  -0.0114 17  ASN B N   
3003 C CA  . ASN B 16  ? 0.4193 0.3761 0.3917 0.0479  0.0297  -0.0021 17  ASN B CA  
3004 C C   . ASN B 16  ? 0.3818 0.3472 0.3799 0.0449  0.0287  0.0051  17  ASN B C   
3005 O O   . ASN B 16  ? 0.4170 0.3911 0.4252 0.0467  0.0327  0.0128  17  ASN B O   
3006 C CB  . ASN B 16  ? 0.3724 0.3373 0.3348 0.0445  0.0200  -0.0023 17  ASN B CB  
3007 C CG  . ASN B 16  ? 0.4685 0.4272 0.4047 0.0494  0.0217  -0.0064 17  ASN B CG  
3008 O OD1 . ASN B 16  ? 0.4304 0.3907 0.3604 0.0548  0.0293  -0.0014 17  ASN B OD1 
3009 N ND2 . ASN B 16  ? 0.4220 0.3727 0.3421 0.0475  0.0147  -0.0156 17  ASN B ND2 
3010 N N   . PHE B 17  ? 0.3770 0.3393 0.3851 0.0403  0.0234  0.0026  18  PHE B N   
3011 C CA  . PHE B 17  ? 0.4006 0.3694 0.4303 0.0377  0.0217  0.0094  18  PHE B CA  
3012 C C   . PHE B 17  ? 0.3957 0.3575 0.4375 0.0411  0.0279  0.0099  18  PHE B C   
3013 O O   . PHE B 17  ? 0.3887 0.3569 0.4475 0.0423  0.0296  0.0170  18  PHE B O   
3014 C CB  . PHE B 17  ? 0.3311 0.3023 0.3652 0.0302  0.0114  0.0083  18  PHE B CB  
3015 C CG  . PHE B 17  ? 0.3079 0.2903 0.3391 0.0270  0.0053  0.0117  18  PHE B CG  
3016 C CD1 . PHE B 17  ? 0.3013 0.2932 0.3448 0.0257  0.0041  0.0202  18  PHE B CD1 
3017 C CD2 . PHE B 17  ? 0.3528 0.3360 0.3688 0.0256  0.0004  0.0064  18  PHE B CD2 
3018 C CE1 . PHE B 17  ? 0.2962 0.2975 0.3370 0.0233  -0.0005 0.0236  18  PHE B CE1 
3019 C CE2 . PHE B 17  ? 0.3556 0.3495 0.3698 0.0234  -0.0050 0.0100  18  PHE B CE2 
3020 C CZ  . PHE B 17  ? 0.3384 0.3412 0.3651 0.0224  -0.0049 0.0188  18  PHE B CZ  
3021 N N   . LYS B 18  ? 0.4115 0.3600 0.4450 0.0429  0.0311  0.0025  19  LYS B N   
3022 C CA  . LYS B 18  ? 0.4224 0.3636 0.4676 0.0470  0.0375  0.0032  19  LYS B CA  
3023 C C   . LYS B 18  ? 0.4011 0.3478 0.4569 0.0538  0.0471  0.0093  19  LYS B C   
3024 O O   . LYS B 18  ? 0.4345 0.3839 0.5094 0.0556  0.0485  0.0143  19  LYS B O   
3025 C CB  . LYS B 18  ? 0.4724 0.3967 0.5036 0.0484  0.0406  -0.0063 19  LYS B CB  
3026 C CG  . LYS B 18  ? 0.4800 0.3949 0.5231 0.0499  0.0432  -0.0067 19  LYS B CG  
3027 C CD  . LYS B 18  ? 0.4819 0.3788 0.5096 0.0491  0.0443  -0.0169 19  LYS B CD  
3028 C CE  . LYS B 18  ? 0.5572 0.4443 0.5695 0.0561  0.0546  -0.0216 19  LYS B CE  
3029 N NZ  . LYS B 18  ? 0.5681 0.4353 0.5675 0.0560  0.0568  -0.0311 19  LYS B NZ  
3030 N N   . PRO B 19  ? 0.4223 0.3705 0.4677 0.0579  0.0540  0.0094  20  PRO B N   
3031 C CA  . PRO B 19  ? 0.4151 0.3693 0.4742 0.0637  0.0638  0.0157  20  PRO B CA  
3032 C C   . PRO B 19  ? 0.4174 0.3869 0.4958 0.0610  0.0595  0.0245  20  PRO B C   
3033 O O   . PRO B 19  ? 0.4096 0.3850 0.5058 0.0646  0.0655  0.0300  20  PRO B O   
3034 C CB  . PRO B 19  ? 0.4707 0.4212 0.5103 0.0679  0.0719  0.0134  20  PRO B CB  
3035 C CG  . PRO B 19  ? 0.4700 0.4184 0.4887 0.0633  0.0629  0.0084  20  PRO B CG  
3036 C CD  . PRO B 19  ? 0.4389 0.3818 0.4592 0.0581  0.0540  0.0035  20  PRO B CD  
3037 N N   . LEU B 20  ? 0.3751 0.3506 0.4508 0.0546  0.0493  0.0260  21  LEU B N   
3038 C CA  . LEU B 20  ? 0.3454 0.3330 0.4377 0.0516  0.0445  0.0339  21  LEU B CA  
3039 C C   . LEU B 20  ? 0.3130 0.3003 0.4241 0.0512  0.0409  0.0367  21  LEU B C   
3040 O O   . LEU B 20  ? 0.3019 0.2978 0.4302 0.0516  0.0404  0.0432  21  LEU B O   
3041 C CB  . LEU B 20  ? 0.3316 0.3240 0.4150 0.0455  0.0354  0.0345  21  LEU B CB  
3042 C CG  . LEU B 20  ? 0.3413 0.3361 0.4076 0.0462  0.0376  0.0337  21  LEU B CG  
3043 C CD1 . LEU B 20  ? 0.3741 0.3737 0.4335 0.0405  0.0279  0.0341  21  LEU B CD1 
3044 C CD2 . LEU B 20  ? 0.3546 0.3566 0.4279 0.0495  0.0453  0.0398  21  LEU B CD2 
3045 N N   . LEU B 21  ? 0.3486 0.3258 0.4565 0.0504  0.0381  0.0319  22  LEU B N   
3046 C CA  . LEU B 21  ? 0.3021 0.2774 0.4263 0.0512  0.0353  0.0349  22  LEU B CA  
3047 C C   . LEU B 21  ? 0.3522 0.3294 0.4920 0.0583  0.0436  0.0377  22  LEU B C   
3048 O O   . LEU B 21  ? 0.3427 0.3257 0.5011 0.0595  0.0409  0.0435  22  LEU B O   
3049 C CB  . LEU B 21  ? 0.3445 0.3065 0.4612 0.0493  0.0323  0.0291  22  LEU B CB  
3050 C CG  . LEU B 21  ? 0.3679 0.3287 0.4765 0.0417  0.0231  0.0276  22  LEU B CG  
3051 C CD1 . LEU B 21  ? 0.4331 0.3866 0.5231 0.0393  0.0234  0.0190  22  LEU B CD1 
3052 C CD2 . LEU B 21  ? 0.3682 0.3216 0.4847 0.0399  0.0183  0.0291  22  LEU B CD2 
3053 N N   . GLU B 22  ? 0.3535 0.3257 0.4860 0.0633  0.0538  0.0337  23  GLU B N   
3054 C CA  . GLU B 22  ? 0.3945 0.3689 0.5432 0.0705  0.0633  0.0365  23  GLU B CA  
3055 C C   . GLU B 22  ? 0.3473 0.3365 0.5102 0.0709  0.0657  0.0433  23  GLU B C   
3056 O O   . GLU B 22  ? 0.3879 0.3848 0.5738 0.0737  0.0666  0.0486  23  GLU B O   
3057 C CB  . GLU B 22  ? 0.4125 0.3751 0.5472 0.0760  0.0747  0.0302  23  GLU B CB  
3058 C CG  . GLU B 22  ? 0.5170 0.4834 0.6658 0.0836  0.0876  0.0333  23  GLU B CG  
3059 C CD  . GLU B 22  ? 0.6072 0.5721 0.7770 0.0892  0.0905  0.0355  23  GLU B CD  
3060 O OE1 . GLU B 22  ? 0.6546 0.6122 0.8251 0.0963  0.1025  0.0334  23  GLU B OE1 
3061 O OE2 . GLU B 22  ? 0.5514 0.5219 0.7364 0.0870  0.0810  0.0396  23  GLU B OE2 
3062 N N   . LYS B 23  ? 0.3390 0.3321 0.4891 0.0680  0.0664  0.0433  24  LYS B N   
3063 C CA  . LYS B 23  ? 0.3457 0.3509 0.5073 0.0682  0.0703  0.0493  24  LYS B CA  
3064 C C   . LYS B 23  ? 0.3273 0.3434 0.5083 0.0641  0.0607  0.0558  24  LYS B C   
3065 O O   . LYS B 23  ? 0.3361 0.3622 0.5372 0.0655  0.0637  0.0609  24  LYS B O   
3066 C CB  . LYS B 23  ? 0.3540 0.3592 0.4949 0.0659  0.0720  0.0480  24  LYS B CB  
3067 C CG  . LYS B 23  ? 0.3722 0.3882 0.5223 0.0653  0.0764  0.0541  24  LYS B CG  
3068 C CD  . LYS B 23  ? 0.3779 0.3905 0.5049 0.0657  0.0813  0.0524  24  LYS B CD  
3069 C CE  . LYS B 23  ? 0.4772 0.4993 0.6124 0.0646  0.0859  0.0587  24  LYS B CE  
3070 N NZ  . LYS B 23  ? 0.5045 0.5220 0.6161 0.0661  0.0917  0.0576  24  LYS B NZ  
3071 N N   . TYR B 24  ? 0.3063 0.3203 0.4816 0.0589  0.0492  0.0555  25  TYR B N   
3072 C CA  . TYR B 24  ? 0.3002 0.3219 0.4884 0.0548  0.0396  0.0612  25  TYR B CA  
3073 C C   . TYR B 24  ? 0.2959 0.3133 0.4940 0.0556  0.0325  0.0620  25  TYR B C   
3074 O O   . TYR B 24  ? 0.2906 0.3116 0.4959 0.0523  0.0233  0.0663  25  TYR B O   
3075 C CB  . TYR B 24  ? 0.3128 0.3353 0.4858 0.0484  0.0327  0.0616  25  TYR B CB  
3076 C CG  . TYR B 24  ? 0.3069 0.3343 0.4716 0.0481  0.0391  0.0623  25  TYR B CG  
3077 C CD1 . TYR B 24  ? 0.3362 0.3731 0.5140 0.0474  0.0412  0.0677  25  TYR B CD1 
3078 C CD2 . TYR B 24  ? 0.2851 0.3067 0.4287 0.0487  0.0429  0.0574  25  TYR B CD2 
3079 C CE1 . TYR B 24  ? 0.3230 0.3629 0.4927 0.0475  0.0481  0.0687  25  TYR B CE1 
3080 C CE2 . TYR B 24  ? 0.3497 0.3746 0.4843 0.0494  0.0491  0.0585  25  TYR B CE2 
3081 C CZ  . TYR B 24  ? 0.3422 0.3758 0.4897 0.0489  0.0522  0.0643  25  TYR B CZ  
3082 O OH  . TYR B 24  ? 0.3827 0.4180 0.5206 0.0497  0.0592  0.0658  25  TYR B OH  
3083 N N   . ASP B 25  ? 0.2779 0.2867 0.4757 0.0602  0.0369  0.0582  26  ASP B N   
3084 C CA  . ASP B 25  ? 0.3403 0.3421 0.5445 0.0618  0.0313  0.0586  26  ASP B CA  
3085 C C   . ASP B 25  ? 0.2982 0.2959 0.4927 0.0555  0.0203  0.0594  26  ASP B C   
3086 O O   . ASP B 25  ? 0.2933 0.2925 0.4971 0.0546  0.0125  0.0641  26  ASP B O   
3087 C CB  . ASP B 25  ? 0.3190 0.3287 0.5487 0.0664  0.0304  0.0642  26  ASP B CB  
3088 C CG  . ASP B 25  ? 0.4003 0.4009 0.6364 0.0718  0.0302  0.0634  26  ASP B CG  
3089 O OD1 . ASP B 25  ? 0.4410 0.4291 0.6627 0.0699  0.0268  0.0600  26  ASP B OD1 
3090 O OD2 . ASP B 25  ? 0.4448 0.4506 0.7010 0.0781  0.0338  0.0662  26  ASP B OD2 
3091 N N   . VAL B 26  ? 0.2784 0.2705 0.4537 0.0512  0.0201  0.0547  27  VAL B N   
3092 C CA  . VAL B 26  ? 0.2750 0.2625 0.4408 0.0452  0.0115  0.0549  27  VAL B CA  
3093 C C   . VAL B 26  ? 0.2868 0.2614 0.4515 0.0464  0.0097  0.0526  27  VAL B C   
3094 O O   . VAL B 26  ? 0.2772 0.2433 0.4356 0.0487  0.0153  0.0467  27  VAL B O   
3095 C CB  . VAL B 26  ? 0.2782 0.2656 0.4264 0.0406  0.0118  0.0507  27  VAL B CB  
3096 C CG1 . VAL B 26  ? 0.2539 0.2372 0.3946 0.0343  0.0039  0.0512  27  VAL B CG1 
3097 C CG2 . VAL B 26  ? 0.2512 0.2501 0.3996 0.0402  0.0145  0.0535  27  VAL B CG2 
3098 N N   . PRO B 27  ? 0.2905 0.2618 0.4597 0.0451  0.0025  0.0569  28  PRO B N   
3099 C CA  . PRO B 27  ? 0.2742 0.2315 0.4416 0.0466  0.0018  0.0550  28  PRO B CA  
3100 C C   . PRO B 27  ? 0.2815 0.2286 0.4331 0.0418  0.0029  0.0484  28  PRO B C   
3101 O O   . PRO B 27  ? 0.3099 0.2460 0.4585 0.0441  0.0072  0.0436  28  PRO B O   
3102 C CB  . PRO B 27  ? 0.2618 0.2176 0.4341 0.0456  -0.0066 0.0617  28  PRO B CB  
3103 C CG  . PRO B 27  ? 0.3314 0.3018 0.5151 0.0466  -0.0092 0.0671  28  PRO B CG  
3104 C CD  . PRO B 27  ? 0.2612 0.2400 0.4385 0.0435  -0.0045 0.0639  28  PRO B CD  
3105 N N   . GLY B 28  ? 0.2637 0.2143 0.4062 0.0353  -0.0007 0.0479  29  GLY B N   
3106 C CA  . GLY B 28  ? 0.2674 0.2104 0.3976 0.0301  -0.0005 0.0416  29  GLY B CA  
3107 C C   . GLY B 28  ? 0.2713 0.2236 0.3935 0.0249  -0.0025 0.0404  29  GLY B C   
3108 O O   . GLY B 28  ? 0.2577 0.2203 0.3826 0.0243  -0.0048 0.0456  29  GLY B O   
3109 N N   . MET B 29  ? 0.2672 0.2153 0.3793 0.0213  -0.0019 0.0333  30  MET B N   
3110 C CA  . MET B 29  ? 0.2617 0.2187 0.3659 0.0172  -0.0040 0.0315  30  MET B CA  
3111 C C   . MET B 29  ? 0.2705 0.2210 0.3673 0.0114  -0.0062 0.0247  30  MET B C   
3112 O O   . MET B 29  ? 0.2844 0.2239 0.3785 0.0118  -0.0039 0.0187  30  MET B O   
3113 C CB  . MET B 29  ? 0.2662 0.2297 0.3654 0.0213  0.0005  0.0292  30  MET B CB  
3114 C CG  . MET B 29  ? 0.2952 0.2670 0.3843 0.0182  -0.0018 0.0272  30  MET B CG  
3115 S SD  . MET B 29  ? 0.3530 0.3284 0.4317 0.0236  0.0044  0.0237  30  MET B SD  
3116 C CE  . MET B 29  ? 0.3642 0.3464 0.4551 0.0293  0.0099  0.0315  30  MET B CE  
3117 N N   . ALA B 30  ? 0.2690 0.2263 0.3635 0.0061  -0.0106 0.0256  31  ALA B N   
3118 C CA  . ALA B 30  ? 0.2702 0.2252 0.3597 0.0001  -0.0135 0.0190  31  ALA B CA  
3119 C C   . ALA B 30  ? 0.2661 0.2333 0.3489 -0.0009 -0.0161 0.0176  31  ALA B C   
3120 O O   . ALA B 30  ? 0.2699 0.2468 0.3549 -0.0012 -0.0178 0.0238  31  ALA B O   
3121 C CB  . ALA B 30  ? 0.2667 0.2176 0.3621 -0.0055 -0.0162 0.0218  31  ALA B CB  
3122 N N   . VAL B 31  ? 0.2786 0.2443 0.3520 -0.0012 -0.0166 0.0095  32  VAL B N   
3123 C CA  . VAL B 31  ? 0.2781 0.2542 0.3429 -0.0011 -0.0196 0.0077  32  VAL B CA  
3124 C C   . VAL B 31  ? 0.2880 0.2633 0.3492 -0.0071 -0.0253 -0.0002 32  VAL B C   
3125 O O   . VAL B 31  ? 0.3032 0.2676 0.3607 -0.0088 -0.0250 -0.0079 32  VAL B O   
3126 C CB  . VAL B 31  ? 0.3107 0.2862 0.3646 0.0055  -0.0151 0.0054  32  VAL B CB  
3127 C CG1 . VAL B 31  ? 0.2979 0.2840 0.3420 0.0064  -0.0180 0.0055  32  VAL B CG1 
3128 C CG2 . VAL B 31  ? 0.3464 0.3223 0.4069 0.0108  -0.0092 0.0122  32  VAL B CG2 
3129 N N   . GLY B 32  ? 0.2806 0.2673 0.3430 -0.0103 -0.0305 0.0014  33  GLY B N   
3130 C CA  . GLY B 32  ? 0.2886 0.2774 0.3509 -0.0164 -0.0370 -0.0055 33  GLY B CA  
3131 C C   . GLY B 32  ? 0.2891 0.2902 0.3434 -0.0152 -0.0423 -0.0065 33  GLY B C   
3132 O O   . GLY B 32  ? 0.2779 0.2881 0.3311 -0.0114 -0.0412 0.0005  33  GLY B O   
3133 N N   . VAL B 33  ? 0.3038 0.3043 0.3522 -0.0185 -0.0485 -0.0155 34  VAL B N   
3134 C CA  . VAL B 33  ? 0.3075 0.3194 0.3488 -0.0181 -0.0557 -0.0176 34  VAL B CA  
3135 C C   . VAL B 33  ? 0.3089 0.3266 0.3623 -0.0265 -0.0635 -0.0220 34  VAL B C   
3136 O O   . VAL B 33  ? 0.3182 0.3266 0.3766 -0.0321 -0.0642 -0.0285 34  VAL B O   
3137 C CB  . VAL B 33  ? 0.3279 0.3335 0.3485 -0.0136 -0.0571 -0.0252 34  VAL B CB  
3138 C CG1 . VAL B 33  ? 0.3408 0.3573 0.3536 -0.0135 -0.0664 -0.0282 34  VAL B CG1 
3139 C CG2 . VAL B 33  ? 0.3266 0.3277 0.3370 -0.0051 -0.0482 -0.0203 34  VAL B CG2 
3140 N N   . ILE B 34  ? 0.3003 0.3330 0.3595 -0.0273 -0.0688 -0.0183 35  ILE B N   
3141 C CA  . ILE B 34  ? 0.3026 0.3435 0.3747 -0.0349 -0.0768 -0.0227 35  ILE B CA  
3142 C C   . ILE B 34  ? 0.3321 0.3849 0.3954 -0.0324 -0.0861 -0.0258 35  ILE B C   
3143 O O   . ILE B 34  ? 0.3244 0.3850 0.3805 -0.0259 -0.0853 -0.0193 35  ILE B O   
3144 C CB  . ILE B 34  ? 0.3272 0.3753 0.4195 -0.0388 -0.0741 -0.0147 35  ILE B CB  
3145 C CG1 . ILE B 34  ? 0.3608 0.4179 0.4691 -0.0471 -0.0816 -0.0195 35  ILE B CG1 
3146 C CG2 . ILE B 34  ? 0.2818 0.3401 0.3729 -0.0328 -0.0712 -0.0041 35  ILE B CG2 
3147 C CD1 . ILE B 34  ? 0.3375 0.3951 0.4660 -0.0526 -0.0765 -0.0138 35  ILE B CD1 
3148 N N   . GLN B 35  ? 0.3297 0.3825 0.3920 -0.0374 -0.0951 -0.0360 36  GLN B N   
3149 C CA  . GLN B 35  ? 0.3892 0.4525 0.4424 -0.0354 -0.1060 -0.0402 36  GLN B CA  
3150 C C   . GLN B 35  ? 0.4088 0.4804 0.4791 -0.0448 -0.1161 -0.0472 36  GLN B C   
3151 O O   . GLN B 35  ? 0.4260 0.4874 0.5013 -0.0519 -0.1165 -0.0550 36  GLN B O   
3152 C CB  . GLN B 35  ? 0.4031 0.4544 0.4292 -0.0301 -0.1075 -0.0474 36  GLN B CB  
3153 C CG  . GLN B 35  ? 0.4536 0.5139 0.4656 -0.0264 -0.1188 -0.0512 36  GLN B CG  
3154 C CD  . GLN B 35  ? 0.5240 0.5691 0.5074 -0.0218 -0.1201 -0.0596 36  GLN B CD  
3155 O OE1 . GLN B 35  ? 0.5541 0.5848 0.5330 -0.0260 -0.1192 -0.0682 36  GLN B OE1 
3156 N NE2 . GLN B 35  ? 0.5000 0.5472 0.4629 -0.0130 -0.1216 -0.0570 36  GLN B NE2 
3157 N N   . ASN B 36  ? 0.4104 0.5005 0.4914 -0.0450 -0.1237 -0.0441 37  ASN B N   
3158 C CA  . ASN B 36  ? 0.3932 0.4943 0.4941 -0.0539 -0.1339 -0.0502 37  ASN B CA  
3159 C C   . ASN B 36  ? 0.3818 0.4755 0.5028 -0.0634 -0.1279 -0.0518 37  ASN B C   
3160 O O   . ASN B 36  ? 0.4149 0.5045 0.5427 -0.0716 -0.1336 -0.0617 37  ASN B O   
3161 C CB  . ASN B 36  ? 0.4643 0.5634 0.5510 -0.0554 -0.1469 -0.0627 37  ASN B CB  
3162 C CG  . ASN B 36  ? 0.5066 0.6140 0.5740 -0.0461 -0.1542 -0.0610 37  ASN B CG  
3163 O OD1 . ASN B 36  ? 0.5111 0.6361 0.5887 -0.0432 -0.1578 -0.0541 37  ASN B OD1 
3164 N ND2 . ASN B 36  ? 0.4952 0.5891 0.5339 -0.0410 -0.1559 -0.0672 37  ASN B ND2 
3165 N N   . ASN B 37  ? 0.4575 0.5477 0.5863 -0.0619 -0.1160 -0.0420 38  ASN B N   
3166 C CA  . ASN B 37  ? 0.4932 0.5752 0.6394 -0.0693 -0.1084 -0.0410 38  ASN B CA  
3167 C C   . ASN B 37  ? 0.5124 0.5732 0.6486 -0.0721 -0.1044 -0.0485 38  ASN B C   
3168 O O   . ASN B 37  ? 0.5167 0.5683 0.6654 -0.0779 -0.0978 -0.0480 38  ASN B O   
3169 C CB  . ASN B 37  ? 0.5455 0.6401 0.7181 -0.0788 -0.1142 -0.0439 38  ASN B CB  
3170 C CG  . ASN B 37  ? 0.5913 0.6822 0.7836 -0.0837 -0.1038 -0.0372 38  ASN B CG  
3171 O OD1 . ASN B 37  ? 0.5461 0.6266 0.7323 -0.0795 -0.0932 -0.0294 38  ASN B OD1 
3172 N ND2 . ASN B 37  ? 0.6255 0.7247 0.8420 -0.0928 -0.1068 -0.0402 38  ASN B ND2 
3173 N N   . LYS B 38  ? 0.4356 0.4872 0.5491 -0.0677 -0.1073 -0.0552 39  LYS B N   
3174 C CA  . LYS B 38  ? 0.4301 0.4605 0.5320 -0.0684 -0.1018 -0.0611 39  LYS B CA  
3175 C C   . LYS B 38  ? 0.3922 0.4138 0.4842 -0.0600 -0.0902 -0.0522 39  LYS B C   
3176 O O   . LYS B 38  ? 0.3769 0.4046 0.4574 -0.0519 -0.0894 -0.0467 39  LYS B O   
3177 C CB  . LYS B 38  ? 0.4177 0.4412 0.4988 -0.0672 -0.1097 -0.0726 39  LYS B CB  
3178 C CG  . LYS B 38  ? 0.5075 0.5443 0.5926 -0.0723 -0.1245 -0.0805 39  LYS B CG  
3179 C CD  . LYS B 38  ? 0.5685 0.6016 0.6252 -0.0657 -0.1318 -0.0870 39  LYS B CD  
3180 C CE  . LYS B 38  ? 0.4137 0.4464 0.4530 -0.0536 -0.1240 -0.0776 39  LYS B CE  
3181 N NZ  . LYS B 38  ? 0.5476 0.5729 0.5571 -0.0459 -0.1272 -0.0824 39  LYS B NZ  
3182 N N   . LYS B 39  ? 0.3439 0.3509 0.4405 -0.0620 -0.0816 -0.0510 40  LYS B N   
3183 C CA  . LYS B 39  ? 0.3410 0.3402 0.4320 -0.0549 -0.0714 -0.0426 40  LYS B CA  
3184 C C   . LYS B 39  ? 0.3772 0.3588 0.4519 -0.0510 -0.0670 -0.0482 40  LYS B C   
3185 O O   . LYS B 39  ? 0.3656 0.3345 0.4391 -0.0560 -0.0678 -0.0570 40  LYS B O   
3186 C CB  . LYS B 39  ? 0.4003 0.3959 0.5081 -0.0585 -0.0645 -0.0353 40  LYS B CB  
3187 C CG  . LYS B 39  ? 0.3957 0.4080 0.5178 -0.0599 -0.0659 -0.0271 40  LYS B CG  
3188 C CD  . LYS B 39  ? 0.4099 0.4182 0.5498 -0.0661 -0.0607 -0.0227 40  LYS B CD  
3189 C CE  . LYS B 39  ? 0.4186 0.4199 0.5567 -0.0609 -0.0518 -0.0121 40  LYS B CE  
3190 N NZ  . LYS B 39  ? 0.3949 0.3906 0.5471 -0.0657 -0.0459 -0.0065 40  LYS B NZ  
3191 N N   . TYR B 40  ? 0.3441 0.3244 0.4067 -0.0420 -0.0619 -0.0430 41  TYR B N   
3192 C CA  . TYR B 40  ? 0.3576 0.3224 0.4055 -0.0367 -0.0561 -0.0468 41  TYR B CA  
3193 C C   . TYR B 40  ? 0.3430 0.3046 0.3953 -0.0310 -0.0468 -0.0368 41  TYR B C   
3194 O O   . TYR B 40  ? 0.3290 0.3006 0.3806 -0.0257 -0.0452 -0.0289 41  TYR B O   
3195 C CB  . TYR B 40  ? 0.3699 0.3365 0.3976 -0.0309 -0.0592 -0.0511 41  TYR B CB  
3196 C CG  . TYR B 40  ? 0.3846 0.3562 0.4071 -0.0361 -0.0705 -0.0604 41  TYR B CG  
3197 C CD1 . TYR B 40  ? 0.3748 0.3646 0.4041 -0.0378 -0.0785 -0.0574 41  TYR B CD1 
3198 C CD2 . TYR B 40  ? 0.5165 0.4744 0.5279 -0.0393 -0.0736 -0.0722 41  TYR B CD2 
3199 C CE1 . TYR B 40  ? 0.3943 0.3899 0.4205 -0.0425 -0.0901 -0.0660 41  TYR B CE1 
3200 C CE2 . TYR B 40  ? 0.5258 0.4882 0.5326 -0.0444 -0.0853 -0.0813 41  TYR B CE2 
3201 C CZ  . TYR B 40  ? 0.5345 0.5164 0.5494 -0.0460 -0.0940 -0.0781 41  TYR B CZ  
3202 O OH  . TYR B 40  ? 0.4703 0.4573 0.4818 -0.0510 -0.1068 -0.0875 41  TYR B OH  
3203 N N   . GLU B 41  ? 0.3473 0.2947 0.4044 -0.0320 -0.0411 -0.0373 42  GLU B N   
3204 C CA  . GLU B 41  ? 0.3340 0.2784 0.3986 -0.0279 -0.0339 -0.0278 42  GLU B CA  
3205 C C   . GLU B 41  ? 0.3447 0.2753 0.4016 -0.0215 -0.0269 -0.0295 42  GLU B C   
3206 O O   . GLU B 41  ? 0.3633 0.2793 0.4168 -0.0236 -0.0253 -0.0368 42  GLU B O   
3207 C CB  . GLU B 41  ? 0.3693 0.3093 0.4485 -0.0341 -0.0331 -0.0250 42  GLU B CB  
3208 C CG  . GLU B 41  ? 0.3361 0.2903 0.4255 -0.0392 -0.0378 -0.0209 42  GLU B CG  
3209 C CD  . GLU B 41  ? 0.4412 0.3894 0.5438 -0.0463 -0.0365 -0.0199 42  GLU B CD  
3210 O OE1 . GLU B 41  ? 0.4487 0.3811 0.5523 -0.0463 -0.0312 -0.0203 42  GLU B OE1 
3211 O OE2 . GLU B 41  ? 0.4644 0.4233 0.5767 -0.0516 -0.0402 -0.0186 42  GLU B OE2 
3212 N N   . MET B 42  ? 0.3352 0.2700 0.3905 -0.0139 -0.0223 -0.0225 43  MET B N   
3213 C CA  . MET B 42  ? 0.3429 0.2671 0.3942 -0.0069 -0.0149 -0.0223 43  MET B CA  
3214 C C   . MET B 42  ? 0.3283 0.2532 0.3921 -0.0037 -0.0110 -0.0124 43  MET B C   
3215 O O   . MET B 42  ? 0.3113 0.2481 0.3807 -0.0030 -0.0126 -0.0047 43  MET B O   
3216 C CB  . MET B 42  ? 0.3619 0.2902 0.4008 -0.0002 -0.0122 -0.0232 43  MET B CB  
3217 C CG  . MET B 42  ? 0.4494 0.3706 0.4712 -0.0007 -0.0141 -0.0340 43  MET B CG  
3218 S SD  . MET B 42  ? 0.6583 0.5868 0.6765 -0.0097 -0.0257 -0.0409 43  MET B SD  
3219 C CE  . MET B 42  ? 0.4553 0.4050 0.4789 -0.0082 -0.0292 -0.0311 43  MET B CE  
3220 N N   . TYR B 43  ? 0.3366 0.2478 0.4038 -0.0015 -0.0063 -0.0128 44  TYR B N   
3221 C CA  . TYR B 43  ? 0.3263 0.2364 0.4043 0.0023  -0.0035 -0.0039 44  TYR B CA  
3222 C C   . TYR B 43  ? 0.3331 0.2375 0.4107 0.0109  0.0033  -0.0032 44  TYR B C   
3223 O O   . TYR B 43  ? 0.3508 0.2432 0.4216 0.0126  0.0073  -0.0102 44  TYR B O   
3224 C CB  . TYR B 43  ? 0.3303 0.2290 0.4146 -0.0023 -0.0040 -0.0034 44  TYR B CB  
3225 C CG  . TYR B 43  ? 0.3242 0.2287 0.4110 -0.0107 -0.0094 -0.0038 44  TYR B CG  
3226 C CD1 . TYR B 43  ? 0.3067 0.2228 0.3993 -0.0117 -0.0122 0.0043  44  TYR B CD1 
3227 C CD2 . TYR B 43  ? 0.3664 0.2650 0.4504 -0.0179 -0.0116 -0.0124 44  TYR B CD2 
3228 C CE1 . TYR B 43  ? 0.3125 0.2343 0.4085 -0.0188 -0.0161 0.0044  44  TYR B CE1 
3229 C CE2 . TYR B 43  ? 0.3440 0.2498 0.4334 -0.0257 -0.0163 -0.0125 44  TYR B CE2 
3230 C CZ  . TYR B 43  ? 0.3343 0.2518 0.4298 -0.0257 -0.0181 -0.0038 44  TYR B CZ  
3231 O OH  . TYR B 43  ? 0.3071 0.2321 0.4089 -0.0326 -0.0217 -0.0032 44  TYR B OH  
3232 N N   . TYR B 44  ? 0.3198 0.2328 0.4056 0.0161  0.0047  0.0051  45  TYR B N   
3233 C CA  . TYR B 44  ? 0.3240 0.2346 0.4135 0.0244  0.0111  0.0071  45  TYR B CA  
3234 C C   . TYR B 44  ? 0.3149 0.2261 0.4182 0.0278  0.0107  0.0157  45  TYR B C   
3235 O O   . TYR B 44  ? 0.3006 0.2197 0.4092 0.0252  0.0057  0.0220  45  TYR B O   
3236 C CB  . TYR B 44  ? 0.3184 0.2411 0.4051 0.0284  0.0138  0.0085  45  TYR B CB  
3237 C CG  . TYR B 44  ? 0.3460 0.2691 0.4170 0.0261  0.0135  0.0009  45  TYR B CG  
3238 C CD1 . TYR B 44  ? 0.3700 0.2817 0.4297 0.0291  0.0188  -0.0069 45  TYR B CD1 
3239 C CD2 . TYR B 44  ? 0.3484 0.2825 0.4150 0.0214  0.0076  0.0017  45  TYR B CD2 
3240 C CE1 . TYR B 44  ? 0.4155 0.3265 0.4585 0.0273  0.0174  -0.0141 45  TYR B CE1 
3241 C CE2 . TYR B 44  ? 0.3839 0.3185 0.4355 0.0199  0.0061  -0.0051 45  TYR B CE2 
3242 C CZ  . TYR B 44  ? 0.4344 0.3574 0.4738 0.0228  0.0106  -0.0130 45  TYR B CZ  
3243 O OH  . TYR B 44  ? 0.4282 0.3505 0.4506 0.0216  0.0081  -0.0199 45  TYR B OH  
3244 N N   . GLY B 45  ? 0.3243 0.2270 0.4329 0.0343  0.0159  0.0161  46  GLY B N   
3245 C CA  . GLY B 45  ? 0.3314 0.2370 0.4539 0.0394  0.0152  0.0245  46  GLY B CA  
3246 C C   . GLY B 45  ? 0.3179 0.2169 0.4435 0.0364  0.0099  0.0289  46  GLY B C   
3247 O O   . GLY B 45  ? 0.3240 0.2108 0.4431 0.0319  0.0095  0.0248  46  GLY B O   
3248 N N   . LEU B 46  ? 0.2682 0.2455 0.4828 0.0063  -0.0965 0.0554  47  LEU B N   
3249 C CA  . LEU B 46  ? 0.2696 0.2253 0.4668 0.0048  -0.1091 0.0654  47  LEU B CA  
3250 C C   . LEU B 46  ? 0.2961 0.2417 0.4574 0.0019  -0.1159 0.0690  47  LEU B C   
3251 O O   . LEU B 46  ? 0.2691 0.2242 0.4284 0.0024  -0.1176 0.0664  47  LEU B O   
3252 C CB  . LEU B 46  ? 0.2744 0.2232 0.4983 0.0080  -0.1247 0.0730  47  LEU B CB  
3253 C CG  . LEU B 46  ? 0.2742 0.2319 0.5384 0.0112  -0.1178 0.0695  47  LEU B CG  
3254 C CD1 . LEU B 46  ? 0.2978 0.2503 0.5929 0.0143  -0.1337 0.0767  47  LEU B CD1 
3255 C CD2 . LEU B 46  ? 0.2881 0.2387 0.5470 0.0095  -0.1084 0.0685  47  LEU B CD2 
3256 N N   . GLN B 47  ? 0.3006 0.2249 0.4327 -0.0011 -0.1187 0.0752  48  GLN B N   
3257 C CA  . GLN B 47  ? 0.3528 0.2629 0.4461 -0.0044 -0.1226 0.0783  48  GLN B CA  
3258 C C   . GLN B 47  ? 0.3842 0.2858 0.4737 -0.0032 -0.1425 0.0845  48  GLN B C   
3259 O O   . GLN B 47  ? 0.3670 0.2698 0.4391 -0.0045 -0.1442 0.0827  48  GLN B O   
3260 C CB  . GLN B 47  ? 0.3725 0.2578 0.4347 -0.0080 -0.1196 0.0840  48  GLN B CB  
3261 C CG  . GLN B 47  ? 0.3296 0.2226 0.3925 -0.0102 -0.0989 0.0770  48  GLN B CG  
3262 C CD  . GLN B 47  ? 0.4105 0.2783 0.4414 -0.0144 -0.0925 0.0821  48  GLN B CD  
3263 O OE1 . GLN B 47  ? 0.3494 0.2211 0.3764 -0.0171 -0.0757 0.0766  48  GLN B OE1 
3264 N NE2 . GLN B 47  ? 0.3980 0.2385 0.4063 -0.0149 -0.1060 0.0929  48  GLN B NE2 
3265 N N   . SER B 48  ? 0.3364 0.2287 0.4435 -0.0007 -0.1586 0.0917  49  SER B N   
3266 C CA  . SER B 48  ? 0.4120 0.3001 0.5226 -0.0003 -0.1765 0.0946  49  SER B CA  
3267 C C   . SER B 48  ? 0.3635 0.2599 0.5139 0.0014  -0.1814 0.0937  49  SER B C   
3268 O O   . SER B 48  ? 0.4059 0.3013 0.5729 0.0030  -0.1776 0.0958  49  SER B O   
3269 C CB  . SER B 48  ? 0.4556 0.3157 0.5211 -0.0045 -0.1874 0.0999  49  SER B CB  
3270 O OG  . SER B 48  ? 0.4742 0.3163 0.5328 -0.0052 -0.1928 0.1060  49  SER B OG  
3271 N N   . VAL B 49  ? 0.3669 0.2699 0.5334 0.0006  -0.1892 0.0907  50  VAL B N   
3272 C CA  . VAL B 49  ? 0.3626 0.2705 0.5669 0.0011  -0.1948 0.0905  50  VAL B CA  
3273 C C   . VAL B 49  ? 0.4738 0.3611 0.6662 -0.0005 -0.2076 0.0975  50  VAL B C   
3274 O O   . VAL B 49  ? 0.4558 0.3458 0.6769 0.0007  -0.2081 0.0989  50  VAL B O   
3275 C CB  . VAL B 49  ? 0.4113 0.3251 0.6317 -0.0005 -0.2014 0.0868  50  VAL B CB  
3276 C CG1 . VAL B 49  ? 0.4786 0.3942 0.7384 -0.0010 -0.2084 0.0874  50  VAL B CG1 
3277 C CG2 . VAL B 49  ? 0.3937 0.3276 0.6266 0.0014  -0.1868 0.0801  50  VAL B CG2 
3278 N N   . GLN B 50  ? 0.4917 0.3569 0.6398 -0.0032 -0.2168 0.1020  51  GLN B N   
3279 C CA  . GLN B 50  ? 0.4634 0.3056 0.5937 -0.0050 -0.2301 0.1089  51  GLN B CA  
3280 C C   . GLN B 50  ? 0.4607 0.2939 0.5801 -0.0036 -0.2214 0.1138  51  GLN B C   
3281 O O   . GLN B 50  ? 0.4830 0.3075 0.6120 -0.0032 -0.2280 0.1184  51  GLN B O   
3282 C CB  . GLN B 50  ? 0.5382 0.3578 0.6223 -0.0087 -0.2417 0.1108  51  GLN B CB  
3283 C CG  . GLN B 50  ? 0.6289 0.4465 0.6775 -0.0095 -0.2299 0.1087  51  GLN B CG  
3284 C CD  . GLN B 50  ? 0.6458 0.4750 0.6965 -0.0104 -0.2300 0.1023  51  GLN B CD  
3285 O OE1 . GLN B 50  ? 0.4780 0.3315 0.5658 -0.0082 -0.2239 0.0970  51  GLN B OE1 
3286 N NE2 . GLN B 50  ? 0.6488 0.4587 0.6572 -0.0136 -0.2351 0.1026  51  GLN B NE2 
3287 N N   . ASP B 51  ? 0.4901 0.3246 0.5922 -0.0029 -0.2062 0.1130  52  ASP B N   
3288 C CA  . ASP B 51  ? 0.4907 0.3140 0.5842 -0.0024 -0.1968 0.1177  52  ASP B CA  
3289 C C   . ASP B 51  ? 0.4361 0.2800 0.5756 0.0011  -0.1853 0.1139  52  ASP B C   
3290 O O   . ASP B 51  ? 0.4462 0.2820 0.5913 0.0016  -0.1812 0.1174  52  ASP B O   
3291 C CB  . ASP B 51  ? 0.4779 0.2858 0.5278 -0.0051 -0.1855 0.1196  52  ASP B CB  
3292 C CG  . ASP B 51  ? 0.5038 0.3311 0.5660 -0.0041 -0.1711 0.1136  52  ASP B CG  
3293 O OD1 . ASP B 51  ? 0.4767 0.3314 0.5797 -0.0011 -0.1645 0.1061  52  ASP B OD1 
3294 O OD2 . ASP B 51  ? 0.5090 0.3300 0.5364 -0.0080 -0.1592 0.1107  52  ASP B OD2 
3295 N N   . LYS B 52  ? 0.3947 0.2638 0.5669 0.0034  -0.1792 0.1065  53  LYS B N   
3296 C CA  . LYS B 52  ? 0.3472 0.2352 0.5618 0.0068  -0.1665 0.1012  53  LYS B CA  
3297 C C   . LYS B 52  ? 0.3576 0.2411 0.5632 0.0066  -0.1509 0.1004  53  LYS B C   
3298 O O   . LYS B 52  ? 0.3542 0.2434 0.5858 0.0080  -0.1417 0.0976  53  LYS B O   
3299 C CB  . LYS B 52  ? 0.4007 0.2908 0.6483 0.0075  -0.1727 0.1023  53  LYS B CB  
3300 C CG  . LYS B 52  ? 0.4227 0.3163 0.6839 0.0061  -0.1871 0.1020  53  LYS B CG  
3301 C CD  . LYS B 52  ? 0.4190 0.3354 0.7112 0.0072  -0.1785 0.0937  53  LYS B CD  
3302 C CE  . LYS B 52  ? 0.5036 0.4247 0.8299 0.0058  -0.1876 0.0929  53  LYS B CE  
3303 N NZ  . LYS B 52  ? 0.5072 0.4110 0.8129 0.0025  -0.2086 0.0986  53  LYS B NZ  
3304 N N   . LYS B 53  ? 0.3827 0.2600 0.5485 0.0025  -0.1432 0.0988  54  LYS B N   
3305 C CA  . LYS B 53  ? 0.3849 0.2619 0.5365 -0.0006 -0.1243 0.0939  54  LYS B CA  
3306 C C   . LYS B 53  ? 0.3380 0.2408 0.4985 -0.0010 -0.1076 0.0810  54  LYS B C   
3307 O O   . LYS B 53  ? 0.3041 0.2155 0.4547 -0.0013 -0.1089 0.0780  54  LYS B O   
3308 C CB  . LYS B 53  ? 0.4131 0.2651 0.5171 -0.0050 -0.1247 0.1002  54  LYS B CB  
3309 C CG  . LYS B 53  ? 0.4981 0.3464 0.5895 -0.0086 -0.1053 0.0964  54  LYS B CG  
3310 C CD  . LYS B 53  ? 0.5527 0.3696 0.5979 -0.0127 -0.1058 0.1050  54  LYS B CD  
3311 C CE  . LYS B 53  ? 0.5852 0.3935 0.6259 -0.0157 -0.0885 0.1042  54  LYS B CE  
3312 N NZ  . LYS B 53  ? 0.5707 0.4044 0.6297 -0.0170 -0.0696 0.0911  54  LYS B NZ  
3313 N N   . ALA B 54  ? 0.3169 0.2303 0.4947 -0.0013 -0.0928 0.0735  55  ALA B N   
3314 C CA  . ALA B 54  ? 0.2685 0.2038 0.4534 -0.0017 -0.0783 0.0612  55  ALA B CA  
3315 C C   . ALA B 54  ? 0.3026 0.2384 0.4570 -0.0051 -0.0730 0.0586  55  ALA B C   
3316 O O   . ALA B 54  ? 0.3125 0.2328 0.4426 -0.0086 -0.0696 0.0623  55  ALA B O   
3317 C CB  . ALA B 54  ? 0.2931 0.2332 0.4939 -0.0025 -0.0649 0.0543  55  ALA B CB  
3318 N N   . VAL B 55  ? 0.2535 0.2065 0.4104 -0.0042 -0.0707 0.0521  56  VAL B N   
3319 C CA  . VAL B 55  ? 0.2669 0.2245 0.4026 -0.0071 -0.0628 0.0473  56  VAL B CA  
3320 C C   . VAL B 55  ? 0.2670 0.2301 0.4080 -0.0094 -0.0488 0.0396  56  VAL B C   
3321 O O   . VAL B 55  ? 0.2490 0.2224 0.4125 -0.0079 -0.0439 0.0333  56  VAL B O   
3322 C CB  . VAL B 55  ? 0.2746 0.2498 0.4151 -0.0052 -0.0636 0.0421  56  VAL B CB  
3323 C CG1 . VAL B 55  ? 0.2480 0.2304 0.3729 -0.0078 -0.0544 0.0359  56  VAL B CG1 
3324 C CG2 . VAL B 55  ? 0.2271 0.1960 0.3611 -0.0037 -0.0776 0.0493  56  VAL B CG2 
3325 N N   . ASN B 56  ? 0.2553 0.2106 0.3766 -0.0132 -0.0419 0.0397  57  ASN B N   
3326 C CA  . ASN B 56  ? 0.2560 0.2158 0.3848 -0.0158 -0.0293 0.0325  57  ASN B CA  
3327 C C   . ASN B 56  ? 0.2877 0.2480 0.4000 -0.0191 -0.0221 0.0298  57  ASN B C   
3328 O O   . ASN B 56  ? 0.2833 0.2425 0.3791 -0.0189 -0.0262 0.0325  57  ASN B O   
3329 C CB  . ASN B 56  ? 0.2919 0.2349 0.4226 -0.0174 -0.0265 0.0375  57  ASN B CB  
3330 C CG  . ASN B 56  ? 0.3496 0.2682 0.4514 -0.0199 -0.0283 0.0480  57  ASN B CG  
3331 O OD1 . ASN B 56  ? 0.3785 0.2885 0.4660 -0.0237 -0.0178 0.0475  57  ASN B OD1 
3332 N ND2 . ASN B 56  ? 0.3885 0.2945 0.4811 -0.0178 -0.0416 0.0573  57  ASN B ND2 
3333 N N   . SER B 57  ? 0.2883 0.2501 0.4075 -0.0221 -0.0109 0.0242  58  SER B N   
3334 C CA  . SER B 57  ? 0.3360 0.3002 0.4469 -0.0250 -0.0029 0.0206  58  SER B CA  
3335 C C   . SER B 57  ? 0.3490 0.2912 0.4320 -0.0279 0.0007  0.0290  58  SER B C   
3336 O O   . SER B 57  ? 0.3826 0.3254 0.4562 -0.0299 0.0068  0.0269  58  SER B O   
3337 C CB  . SER B 57  ? 0.2993 0.2706 0.4300 -0.0276 0.0072  0.0122  58  SER B CB  
3338 O OG  . SER B 57  ? 0.3077 0.2640 0.4413 -0.0297 0.0129  0.0159  58  SER B OG  
3339 N N   . SER B 58  ? 0.3766 0.2976 0.4450 -0.0283 -0.0027 0.0383  59  SER B N   
3340 C CA  . SER B 58  ? 0.3603 0.2556 0.3951 -0.0310 -0.0005 0.0467  59  SER B CA  
3341 C C   . SER B 58  ? 0.3862 0.2762 0.4001 -0.0290 -0.0143 0.0522  59  SER B C   
3342 O O   . SER B 58  ? 0.3893 0.2573 0.3711 -0.0315 -0.0134 0.0581  59  SER B O   
3343 C CB  . SER B 58  ? 0.3672 0.2377 0.3914 -0.0327 0.0015  0.0550  59  SER B CB  
3344 O OG  . SER B 58  ? 0.4208 0.2928 0.4629 -0.0353 0.0158  0.0505  59  SER B OG  
3345 N N   . THR B 59  ? 0.3397 0.2477 0.3703 -0.0249 -0.0264 0.0502  60  THR B N   
3346 C CA  . THR B 59  ? 0.3343 0.2372 0.3504 -0.0229 -0.0409 0.0556  60  THR B CA  
3347 C C   . THR B 59  ? 0.3454 0.2488 0.3427 -0.0246 -0.0374 0.0532  60  THR B C   
3348 O O   . THR B 59  ? 0.3391 0.2616 0.3497 -0.0246 -0.0295 0.0451  60  THR B O   
3349 C CB  . THR B 59  ? 0.3092 0.2326 0.3532 -0.0181 -0.0513 0.0530  60  THR B CB  
3350 O OG1 . THR B 59  ? 0.3131 0.2344 0.3756 -0.0166 -0.0536 0.0550  60  THR B OG1 
3351 C CG2 . THR B 59  ? 0.3001 0.2192 0.3345 -0.0161 -0.0670 0.0584  60  THR B CG2 
3352 N N   . ILE B 60  ? 0.3571 0.2380 0.3227 -0.0260 -0.0444 0.0603  61  ILE B N   
3353 C CA  . ILE B 60  ? 0.3566 0.2330 0.3001 -0.0281 -0.0411 0.0586  61  ILE B CA  
3354 C C   . ILE B 60  ? 0.3616 0.2471 0.3081 -0.0250 -0.0571 0.0594  61  ILE B C   
3355 O O   . ILE B 60  ? 0.3741 0.2489 0.3160 -0.0233 -0.0731 0.0661  61  ILE B O   
3356 C CB  . ILE B 60  ? 0.3955 0.2367 0.2970 -0.0324 -0.0364 0.0652  61  ILE B CB  
3357 C CG1 . ILE B 60  ? 0.4249 0.2573 0.3265 -0.0358 -0.0172 0.0640  61  ILE B CG1 
3358 C CG2 . ILE B 60  ? 0.4321 0.2657 0.3085 -0.0344 -0.0343 0.0635  61  ILE B CG2 
3359 C CD1 . ILE B 60  ? 0.4760 0.2691 0.3359 -0.0398 -0.0123 0.0723  61  ILE B CD1 
3360 N N   . PHE B 61  ? 0.3336 0.2380 0.2892 -0.0242 -0.0532 0.0528  62  PHE B N   
3361 C CA  . PHE B 61  ? 0.3081 0.2232 0.2697 -0.0214 -0.0657 0.0526  62  PHE B CA  
3362 C C   . PHE B 61  ? 0.3490 0.2546 0.2851 -0.0239 -0.0634 0.0517  62  PHE B C   
3363 O O   . PHE B 61  ? 0.3617 0.2649 0.2887 -0.0268 -0.0484 0.0479  62  PHE B O   
3364 C CB  . PHE B 61  ? 0.2871 0.2331 0.2826 -0.0179 -0.0632 0.0455  62  PHE B CB  
3365 C CG  . PHE B 61  ? 0.2866 0.2434 0.3091 -0.0151 -0.0655 0.0449  62  PHE B CG  
3366 C CD1 . PHE B 61  ? 0.2846 0.2449 0.3172 -0.0161 -0.0549 0.0415  62  PHE B CD1 
3367 C CD2 . PHE B 61  ? 0.2814 0.2459 0.3221 -0.0114 -0.0772 0.0469  62  PHE B CD2 
3368 C CE1 . PHE B 61  ? 0.2866 0.2560 0.3437 -0.0136 -0.0562 0.0401  62  PHE B CE1 
3369 C CE2 . PHE B 61  ? 0.2947 0.2686 0.3615 -0.0088 -0.0772 0.0456  62  PHE B CE2 
3370 C CZ  . PHE B 61  ? 0.2602 0.2359 0.3336 -0.0099 -0.0667 0.0421  62  PHE B CZ  
3371 N N   . GLU B 62  ? 0.3347 0.2353 0.2623 -0.0229 -0.0779 0.0547  63  GLU B N   
3372 C CA  . GLU B 62  ? 0.3193 0.2151 0.2279 -0.0247 -0.0764 0.0524  63  GLU B CA  
3373 C C   . GLU B 62  ? 0.3414 0.2661 0.2758 -0.0226 -0.0682 0.0449  63  GLU B C   
3374 O O   . GLU B 62  ? 0.3261 0.2730 0.2905 -0.0190 -0.0709 0.0427  63  GLU B O   
3375 C CB  . GLU B 62  ? 0.3892 0.2722 0.2848 -0.0241 -0.0961 0.0573  63  GLU B CB  
3376 C CG  . GLU B 62  ? 0.4586 0.3080 0.3217 -0.0265 -0.1066 0.0653  63  GLU B CG  
3377 C CD  . GLU B 62  ? 0.5720 0.4067 0.4228 -0.0261 -0.1296 0.0701  63  GLU B CD  
3378 O OE1 . GLU B 62  ? 0.5502 0.4010 0.4187 -0.0241 -0.1369 0.0671  63  GLU B OE1 
3379 O OE2 . GLU B 62  ? 0.5942 0.3997 0.4171 -0.0278 -0.1414 0.0772  63  GLU B OE2 
3380 N N   . LEU B 63  ? 0.3428 0.2654 0.2645 -0.0249 -0.0579 0.0411  64  LEU B N   
3381 C CA  . LEU B 63  ? 0.2954 0.2427 0.2392 -0.0231 -0.0504 0.0345  64  LEU B CA  
3382 C C   . LEU B 63  ? 0.3337 0.2846 0.2740 -0.0223 -0.0567 0.0336  64  LEU B C   
3383 O O   . LEU B 63  ? 0.2814 0.2532 0.2415 -0.0200 -0.0533 0.0292  64  LEU B O   
3384 C CB  . LEU B 63  ? 0.3124 0.2588 0.2541 -0.0259 -0.0322 0.0300  64  LEU B CB  
3385 C CG  . LEU B 63  ? 0.3170 0.2610 0.2657 -0.0274 -0.0222 0.0294  64  LEU B CG  
3386 C CD1 . LEU B 63  ? 0.2771 0.2209 0.2283 -0.0303 -0.0044 0.0244  64  LEU B CD1 
3387 C CD2 . LEU B 63  ? 0.2732 0.2390 0.2523 -0.0239 -0.0266 0.0274  64  LEU B CD2 
3388 N N   . GLY B 64  ? 0.3348 0.2645 0.2494 -0.0241 -0.0663 0.0374  65  GLY B N   
3389 C CA  . GLY B 64  ? 0.3515 0.2835 0.2629 -0.0238 -0.0718 0.0358  65  GLY B CA  
3390 C C   . GLY B 64  ? 0.3274 0.2658 0.2387 -0.0251 -0.0564 0.0302  65  GLY B C   
3391 O O   . GLY B 64  ? 0.3554 0.2813 0.2515 -0.0284 -0.0428 0.0286  65  GLY B O   
3392 N N   . SER B 65  ? 0.3160 0.2744 0.2472 -0.0224 -0.0578 0.0272  66  SER B N   
3393 C CA  . SER B 65  ? 0.3166 0.2823 0.2513 -0.0230 -0.0458 0.0223  66  SER B CA  
3394 C C   . SER B 65  ? 0.3113 0.2892 0.2624 -0.0229 -0.0317 0.0187  66  SER B C   
3395 O O   . SER B 65  ? 0.2700 0.2497 0.2233 -0.0241 -0.0204 0.0148  66  SER B O   
3396 C CB  . SER B 65  ? 0.3406 0.3253 0.2951 -0.0196 -0.0519 0.0209  66  SER B CB  
3397 O OG  . SER B 65  ? 0.4465 0.4174 0.3839 -0.0212 -0.0595 0.0218  66  SER B OG  
3398 N N   . VAL B 66  ? 0.2429 0.2292 0.2078 -0.0215 -0.0324 0.0194  67  VAL B N   
3399 C CA  . VAL B 66  ? 0.2419 0.2368 0.2215 -0.0220 -0.0202 0.0156  67  VAL B CA  
3400 C C   . VAL B 66  ? 0.2580 0.2314 0.2181 -0.0268 -0.0070 0.0152  67  VAL B C   
3401 O O   . VAL B 66  ? 0.2655 0.2438 0.2386 -0.0280 0.0058  0.0112  67  VAL B O   
3402 C CB  . VAL B 66  ? 0.2719 0.2781 0.2688 -0.0198 -0.0241 0.0160  67  VAL B CB  
3403 C CG1 . VAL B 66  ? 0.2351 0.2459 0.2451 -0.0212 -0.0129 0.0121  67  VAL B CG1 
3404 C CG2 . VAL B 66  ? 0.2602 0.2880 0.2776 -0.0153 -0.0321 0.0148  67  VAL B CG2 
3405 N N   . SER B 67  ? 0.2813 0.2292 0.2099 -0.0296 -0.0097 0.0192  68  SER B N   
3406 C CA  . SER B 67  ? 0.3191 0.2419 0.2230 -0.0344 0.0048  0.0187  68  SER B CA  
3407 C C   . SER B 67  ? 0.3364 0.2628 0.2465 -0.0356 0.0179  0.0134  68  SER B C   
3408 O O   . SER B 67  ? 0.3331 0.2483 0.2400 -0.0389 0.0355  0.0109  68  SER B O   
3409 C CB  . SER B 67  ? 0.3832 0.2753 0.2464 -0.0371 -0.0028 0.0237  68  SER B CB  
3410 O OG  . SER B 67  ? 0.4035 0.2915 0.2626 -0.0357 -0.0174 0.0293  68  SER B OG  
3411 N N   . LYS B 68  ? 0.3245 0.2648 0.2440 -0.0330 0.0105  0.0118  69  LYS B N   
3412 C CA  . LYS B 68  ? 0.2914 0.2347 0.2178 -0.0338 0.0218  0.0071  69  LYS B CA  
3413 C C   . LYS B 68  ? 0.3054 0.2663 0.2647 -0.0331 0.0338  0.0027  69  LYS B C   
3414 O O   . LYS B 68  ? 0.3000 0.2574 0.2650 -0.0350 0.0479  -0.0011 69  LYS B O   
3415 C CB  . LYS B 68  ? 0.3045 0.2619 0.2390 -0.0306 0.0102  0.0068  69  LYS B CB  
3416 C CG  . LYS B 68  ? 0.3683 0.3084 0.2743 -0.0316 -0.0028 0.0101  69  LYS B CG  
3417 C CD  . LYS B 68  ? 0.3567 0.3137 0.2778 -0.0282 -0.0131 0.0095  69  LYS B CD  
3418 C CE  . LYS B 68  ? 0.3996 0.3388 0.2956 -0.0297 -0.0256 0.0116  69  LYS B CE  
3419 N NZ  . LYS B 68  ? 0.4099 0.3420 0.2971 -0.0292 -0.0405 0.0167  69  LYS B NZ  
3420 N N   . LEU B 69  ? 0.2438 0.2224 0.2257 -0.0306 0.0284  0.0030  70  LEU B N   
3421 C CA  . LEU B 69  ? 0.2688 0.2616 0.2816 -0.0304 0.0379  -0.0014 70  LEU B CA  
3422 C C   . LEU B 69  ? 0.2803 0.2538 0.2866 -0.0352 0.0563  -0.0027 70  LEU B C   
3423 O O   . LEU B 69  ? 0.2952 0.2740 0.3248 -0.0363 0.0690  -0.0071 70  LEU B O   
3424 C CB  . LEU B 69  ? 0.2287 0.2406 0.2625 -0.0273 0.0277  -0.0013 70  LEU B CB  
3425 C CG  . LEU B 69  ? 0.2534 0.2818 0.2921 -0.0227 0.0115  0.0003  70  LEU B CG  
3426 C CD1 . LEU B 69  ? 0.2158 0.2587 0.2718 -0.0203 0.0044  -0.0005 70  LEU B CD1 
3427 C CD2 . LEU B 69  ? 0.2225 0.2636 0.2742 -0.0204 0.0105  -0.0019 70  LEU B CD2 
3428 N N   . PHE B 70  ? 0.3318 0.2824 0.3086 -0.0380 0.0581  0.0012  71  PHE B N   
3429 C CA  . PHE B 70  ? 0.3260 0.2550 0.2935 -0.0428 0.0779  0.0004  71  PHE B CA  
3430 C C   . PHE B 70  ? 0.3531 0.2619 0.3006 -0.0460 0.0924  -0.0016 71  PHE B C   
3431 O O   . PHE B 70  ? 0.3431 0.2434 0.3005 -0.0492 0.1129  -0.0052 71  PHE B O   
3432 C CB  . PHE B 70  ? 0.3758 0.2840 0.3155 -0.0447 0.0754  0.0060  71  PHE B CB  
3433 C CG  . PHE B 70  ? 0.3564 0.2826 0.3193 -0.0421 0.0658  0.0068  71  PHE B CG  
3434 C CD1 . PHE B 70  ? 0.3757 0.3132 0.3702 -0.0428 0.0758  0.0029  71  PHE B CD1 
3435 C CD2 . PHE B 70  ? 0.3864 0.3189 0.3428 -0.0390 0.0467  0.0109  71  PHE B CD2 
3436 C CE1 . PHE B 70  ? 0.3058 0.2588 0.3207 -0.0406 0.0669  0.0027  71  PHE B CE1 
3437 C CE2 . PHE B 70  ? 0.3469 0.2949 0.3246 -0.0367 0.0395  0.0110  71  PHE B CE2 
3438 C CZ  . PHE B 70  ? 0.3220 0.2799 0.3273 -0.0376 0.0493  0.0067  71  PHE B CZ  
3439 N N   . THR B 71  ? 0.3570 0.2576 0.2786 -0.0455 0.0826  0.0002  72  THR B N   
3440 C CA  . THR B 71  ? 0.4019 0.2845 0.3054 -0.0484 0.0952  -0.0027 72  THR B CA  
3441 C C   . THR B 71  ? 0.3598 0.2635 0.3030 -0.0469 0.1049  -0.0086 72  THR B C   
3442 O O   . THR B 71  ? 0.3976 0.2879 0.3424 -0.0501 0.1257  -0.0125 72  THR B O   
3443 C CB  . THR B 71  ? 0.4020 0.2764 0.2763 -0.0475 0.0792  -0.0003 72  THR B CB  
3444 O OG1 . THR B 71  ? 0.4331 0.2876 0.2734 -0.0487 0.0678  0.0056  72  THR B OG1 
3445 C CG2 . THR B 71  ? 0.4734 0.3262 0.3252 -0.0509 0.0923  -0.0040 72  THR B CG2 
3446 N N   . ALA B 72  ? 0.3117 0.2469 0.2874 -0.0420 0.0903  -0.0092 73  ALA B N   
3447 C CA  . ALA B 72  ? 0.3410 0.2971 0.3563 -0.0399 0.0957  -0.0139 73  ALA B CA  
3448 C C   . ALA B 72  ? 0.3514 0.3094 0.3956 -0.0420 0.1121  -0.0173 73  ALA B C   
3449 O O   . ALA B 72  ? 0.3046 0.2623 0.3698 -0.0432 0.1274  -0.0217 73  ALA B O   
3450 C CB  . ALA B 72  ? 0.2605 0.2465 0.2997 -0.0343 0.0756  -0.0128 73  ALA B CB  
3451 N N   . THR B 73  ? 0.3035 0.2637 0.3521 -0.0423 0.1094  -0.0157 74  THR B N   
3452 C CA  . THR B 73  ? 0.2908 0.2521 0.3688 -0.0445 0.1248  -0.0191 74  THR B CA  
3453 C C   . THR B 73  ? 0.3539 0.2856 0.4147 -0.0500 0.1508  -0.0205 74  THR B C   
3454 O O   . THR B 73  ? 0.3469 0.2798 0.4391 -0.0518 0.1685  -0.0252 74  THR B O   
3455 C CB  . THR B 73  ? 0.3176 0.2830 0.3981 -0.0443 0.1172  -0.0167 74  THR B CB  
3456 O OG1 . THR B 73  ? 0.2903 0.2806 0.3835 -0.0394 0.0946  -0.0158 74  THR B OG1 
3457 C CG2 . THR B 73  ? 0.3264 0.2951 0.4425 -0.0466 0.1318  -0.0208 74  THR B CG2 
3458 N N   . ALA B 74  ? 0.3752 0.2781 0.3860 -0.0529 0.1538  -0.0167 75  ALA B N   
3459 C CA  . ALA B 74  ? 0.4299 0.2995 0.4167 -0.0584 0.1798  -0.0181 75  ALA B CA  
3460 C C   . ALA B 74  ? 0.4260 0.2935 0.4215 -0.0591 0.1922  -0.0231 75  ALA B C   
3461 O O   . ALA B 74  ? 0.4670 0.3208 0.4744 -0.0626 0.2178  -0.0272 75  ALA B O   
3462 C CB  . ALA B 74  ? 0.4394 0.2759 0.3659 -0.0612 0.1769  -0.0124 75  ALA B CB  
3463 N N   . GLY B 75  ? 0.4305 0.3114 0.4232 -0.0556 0.1753  -0.0229 76  GLY B N   
3464 C CA  . GLY B 75  ? 0.4264 0.3099 0.4347 -0.0554 0.1850  -0.0277 76  GLY B CA  
3465 C C   . GLY B 75  ? 0.3998 0.3078 0.4686 -0.0537 0.1930  -0.0324 76  GLY B C   
3466 O O   . GLY B 75  ? 0.4082 0.3078 0.4943 -0.0560 0.2146  -0.0371 76  GLY B O   
3467 N N   . GLY B 76  ? 0.3735 0.3108 0.4759 -0.0497 0.1756  -0.0312 77  GLY B N   
3468 C CA  . GLY B 76  ? 0.3807 0.3398 0.5409 -0.0482 0.1802  -0.0355 77  GLY B CA  
3469 C C   . GLY B 76  ? 0.4069 0.3505 0.5831 -0.0525 0.2049  -0.0387 77  GLY B C   
3470 O O   . GLY B 76  ? 0.3843 0.3305 0.5946 -0.0498 0.2098  -0.0434 77  GLY B O   
3471 N N   . TYR B 77  ? 0.4116 0.3343 0.5563 -0.0564 0.2133  -0.0358 78  TYR B N   
3472 C CA  . TYR B 77  ? 0.4159 0.3189 0.5664 -0.0576 0.2306  -0.0386 78  TYR B CA  
3473 C C   . TYR B 77  ? 0.5152 0.3878 0.6460 -0.0591 0.2514  -0.0424 78  TYR B C   
3474 O O   . TYR B 77  ? 0.4957 0.3627 0.6562 -0.0578 0.2636  -0.0477 78  TYR B O   
3475 C CB  . TYR B 77  ? 0.4413 0.3289 0.5599 -0.0612 0.2328  -0.0336 78  TYR B CB  
3476 C CG  . TYR B 77  ? 0.5090 0.3769 0.6321 -0.0621 0.2495  -0.0359 78  TYR B CG  
3477 C CD1 . TYR B 77  ? 0.5366 0.3678 0.6257 -0.0645 0.2702  -0.0373 78  TYR B CD1 
3478 C CD2 . TYR B 77  ? 0.4943 0.3786 0.6534 -0.0606 0.2442  -0.0368 78  TYR B CD2 
3479 C CE1 . TYR B 77  ? 0.6015 0.4136 0.6945 -0.0652 0.2866  -0.0395 78  TYR B CE1 
3480 C CE2 . TYR B 77  ? 0.5087 0.3749 0.6728 -0.0613 0.2601  -0.0390 78  TYR B CE2 
3481 C CZ  . TYR B 77  ? 0.5856 0.4160 0.7172 -0.0634 0.2819  -0.0402 78  TYR B CZ  
3482 O OH  . TYR B 77  ? 0.6721 0.4837 0.8092 -0.0639 0.2989  -0.0425 78  TYR B OH  
3483 N N   . ALA B 78  ? 0.4840 0.3346 0.5641 -0.0621 0.2553  -0.0400 79  ALA B N   
3484 C CA  . ALA B 78  ? 0.5100 0.3302 0.5680 -0.0639 0.2736  -0.0443 79  ALA B CA  
3485 C C   . ALA B 78  ? 0.5554 0.3917 0.6558 -0.0607 0.2742  -0.0496 79  ALA B C   
3486 O O   . ALA B 78  ? 0.6086 0.4265 0.7193 -0.0612 0.2916  -0.0549 79  ALA B O   
3487 C CB  . ALA B 78  ? 0.5750 0.3698 0.5690 -0.0675 0.2721  -0.0408 79  ALA B CB  
3488 N N   . LYS B 79  ? 0.4653 0.3341 0.5905 -0.0574 0.2554  -0.0482 80  LYS B N   
3489 C CA  . LYS B 79  ? 0.5003 0.3845 0.6652 -0.0538 0.2530  -0.0522 80  LYS B CA  
3490 C C   . LYS B 79  ? 0.5070 0.3982 0.7231 -0.0511 0.2572  -0.0562 80  LYS B C   
3491 O O   . LYS B 79  ? 0.4914 0.3709 0.7262 -0.0508 0.2699  -0.0609 80  LYS B O   
3492 C CB  . LYS B 79  ? 0.4512 0.3689 0.6321 -0.0502 0.2298  -0.0491 80  LYS B CB  
3493 C CG  . LYS B 79  ? 0.4834 0.4163 0.7012 -0.0460 0.2242  -0.0520 80  LYS B CG  
3494 C CD  . LYS B 79  ? 0.4565 0.4166 0.7260 -0.0411 0.2081  -0.0521 80  LYS B CD  
3495 C CE  . LYS B 79  ? 0.4645 0.4394 0.7651 -0.0368 0.1983  -0.0532 80  LYS B CE  
3496 N NZ  . LYS B 79  ? 0.4974 0.4960 0.8399 -0.0320 0.1784  -0.0523 80  LYS B NZ  
3497 N N   . ASN B 80  ? 0.4649 0.3737 0.7045 -0.0494 0.2465  -0.0547 81  ASN B N   
3498 C CA  . ASN B 80  ? 0.4505 0.3685 0.7411 -0.0464 0.2459  -0.0584 81  ASN B CA  
3499 C C   . ASN B 80  ? 0.4844 0.3742 0.7752 -0.0489 0.2697  -0.0622 81  ASN B C   
3500 O O   . ASN B 80  ? 0.5063 0.3994 0.8404 -0.0467 0.2724  -0.0660 81  ASN B O   
3501 C CB  . ASN B 80  ? 0.4633 0.4101 0.7793 -0.0435 0.2234  -0.0560 81  ASN B CB  
3502 C CG  . ASN B 80  ? 0.4544 0.4299 0.7873 -0.0393 0.1991  -0.0539 81  ASN B CG  
3503 O OD1 . ASN B 80  ? 0.4681 0.4530 0.8360 -0.0359 0.1919  -0.0561 81  ASN B OD1 
3504 N ND2 . ASN B 80  ? 0.4374 0.4252 0.7449 -0.0396 0.1861  -0.0495 81  ASN B ND2 
3505 N N   . LYS B 81  ? 0.5113 0.3716 0.7543 -0.0533 0.2866  -0.0612 82  LYS B N   
3506 C CA  . LYS B 81  ? 0.5771 0.4049 0.8151 -0.0557 0.3122  -0.0653 82  LYS B CA  
3507 C C   . LYS B 81  ? 0.6085 0.4076 0.8225 -0.0584 0.3304  -0.0687 82  LYS B C   
3508 O O   . LYS B 81  ? 0.6657 0.4302 0.8582 -0.0615 0.3532  -0.0715 82  LYS B O   
3509 C CB  . LYS B 81  ? 0.6031 0.4122 0.8032 -0.0587 0.3197  -0.0622 82  LYS B CB  
3510 C CG  . LYS B 81  ? 0.5880 0.4197 0.8178 -0.0566 0.3074  -0.0604 82  LYS B CG  
3511 C CD  . LYS B 81  ? 0.7050 0.5118 0.9211 -0.0586 0.3251  -0.0608 82  LYS B CD  
3512 C CE  . LYS B 81  ? 0.7293 0.5041 0.8775 -0.0630 0.3348  -0.0567 82  LYS B CE  
3513 N NZ  . LYS B 81  ? 0.7858 0.5366 0.9195 -0.0646 0.3504  -0.0564 82  LYS B NZ  
3514 N N   . GLY B 82  ? 0.6085 0.4199 0.8252 -0.0573 0.3210  -0.0686 83  GLY B N   
3515 C CA  . GLY B 82  ? 0.5759 0.3619 0.7760 -0.0599 0.3373  -0.0723 83  GLY B CA  
3516 C C   . GLY B 82  ? 0.6568 0.4073 0.7891 -0.0653 0.3491  -0.0711 83  GLY B C   
3517 O O   . GLY B 82  ? 0.6690 0.3897 0.7837 -0.0686 0.3672  -0.0750 83  GLY B O   
3518 N N   . LYS B 83  ? 0.6290 0.3800 0.7213 -0.0665 0.3384  -0.0655 84  LYS B N   
3519 C CA  . LYS B 83  ? 0.6578 0.3736 0.6819 -0.0713 0.3450  -0.0636 84  LYS B CA  
3520 C C   . LYS B 83  ? 0.6992 0.4198 0.7012 -0.0719 0.3341  -0.0627 84  LYS B C   
3521 O O   . LYS B 83  ? 0.7128 0.4003 0.6658 -0.0761 0.3421  -0.0635 84  LYS B O   
3522 C CB  . LYS B 83  ? 0.7078 0.4184 0.6959 -0.0725 0.3369  -0.0576 84  LYS B CB  
3523 C CG  . LYS B 83  ? 0.7175 0.4181 0.7194 -0.0724 0.3495  -0.0584 84  LYS B CG  
3524 C CD  . LYS B 83  ? 0.8209 0.4805 0.8079 -0.0756 0.3764  -0.0637 84  LYS B CD  
3525 C CE  . LYS B 83  ? 0.8353 0.4744 0.8127 -0.0765 0.3894  -0.0632 84  LYS B CE  
3526 N NZ  . LYS B 83  ? 0.8413 0.4373 0.8019 -0.0798 0.4172  -0.0686 84  LYS B NZ  
3527 N N   . ILE B 84  ? 0.6704 0.4302 0.7070 -0.0677 0.3154  -0.0611 85  ILE B N   
3528 C CA  . ILE B 84  ? 0.5881 0.3564 0.6140 -0.0672 0.3057  -0.0609 85  ILE B CA  
3529 C C   . ILE B 84  ? 0.5521 0.3566 0.6400 -0.0620 0.2964  -0.0628 85  ILE B C   
3530 O O   . ILE B 84  ? 0.5401 0.3663 0.6744 -0.0586 0.2916  -0.0629 85  ILE B O   
3531 C CB  . ILE B 84  ? 0.5982 0.3750 0.5864 -0.0675 0.2867  -0.0549 85  ILE B CB  
3532 C CG1 . ILE B 84  ? 0.5644 0.3764 0.5850 -0.0640 0.2705  -0.0504 85  ILE B CG1 
3533 C CG2 . ILE B 84  ? 0.6414 0.3779 0.5609 -0.0725 0.2915  -0.0526 85  ILE B CG2 
3534 C CD1 . ILE B 84  ? 0.5595 0.3809 0.5485 -0.0645 0.2522  -0.0441 85  ILE B CD1 
3535 N N   . SER B 85  ? 0.5388 0.3475 0.6254 -0.0615 0.2929  -0.0642 86  SER B N   
3536 C CA  . SER B 85  ? 0.5088 0.3531 0.6425 -0.0561 0.2777  -0.0639 86  SER B CA  
3537 C C   . SER B 85  ? 0.4888 0.3469 0.5975 -0.0552 0.2614  -0.0602 86  SER B C   
3538 O O   . SER B 85  ? 0.5076 0.3415 0.5655 -0.0591 0.2664  -0.0605 86  SER B O   
3539 C CB  . SER B 85  ? 0.5129 0.3490 0.6724 -0.0559 0.2893  -0.0690 86  SER B CB  
3540 O OG  . SER B 85  ? 0.5698 0.4350 0.7608 -0.0511 0.2732  -0.0679 86  SER B OG  
3541 N N   . PHE B 86  ? 0.4297 0.3245 0.5718 -0.0501 0.2411  -0.0568 87  PHE B N   
3542 C CA  . PHE B 86  ? 0.4014 0.3089 0.5222 -0.0493 0.2270  -0.0535 87  PHE B CA  
3543 C C   . PHE B 86  ? 0.4353 0.3363 0.5488 -0.0492 0.2304  -0.0565 87  PHE B C   
3544 O O   . PHE B 86  ? 0.4275 0.3297 0.5130 -0.0476 0.2117  -0.0537 87  PHE B O   
3545 C CB  . PHE B 86  ? 0.3284 0.2734 0.4836 -0.0432 0.2003  -0.0487 87  PHE B CB  
3546 C CG  . PHE B 86  ? 0.3644 0.3150 0.5161 -0.0433 0.1920  -0.0452 87  PHE B CG  
3547 C CD1 . PHE B 86  ? 0.4086 0.3324 0.5168 -0.0480 0.2009  -0.0443 87  PHE B CD1 
3548 C CD2 . PHE B 86  ? 0.4044 0.3850 0.5949 -0.0388 0.1748  -0.0429 87  PHE B CD2 
3549 C CE1 . PHE B 86  ? 0.4365 0.3655 0.5431 -0.0480 0.1934  -0.0410 87  PHE B CE1 
3550 C CE2 . PHE B 86  ? 0.3747 0.3600 0.5625 -0.0391 0.1674  -0.0404 87  PHE B CE2 
3551 C CZ  . PHE B 86  ? 0.4072 0.3675 0.5548 -0.0436 0.1771  -0.0394 87  PHE B CZ  
3552 N N   . ASP B 87  ? 0.4453 0.3350 0.5788 -0.0493 0.2432  -0.0612 88  ASP B N   
3553 C CA  . ASP B 87  ? 0.4826 0.3614 0.6072 -0.0501 0.2492  -0.0647 88  ASP B CA  
3554 C C   . ASP B 87  ? 0.5050 0.3414 0.5729 -0.0569 0.2667  -0.0685 88  ASP B C   
3555 O O   . ASP B 87  ? 0.5939 0.4175 0.6472 -0.0585 0.2717  -0.0720 88  ASP B O   
3556 C CB  . ASP B 87  ? 0.5183 0.4037 0.6925 -0.0475 0.2539  -0.0675 88  ASP B CB  
3557 C CG  . ASP B 87  ? 0.5721 0.4952 0.7950 -0.0404 0.2323  -0.0635 88  ASP B CG  
3558 O OD1 . ASP B 87  ? 0.5153 0.4594 0.7332 -0.0375 0.2149  -0.0593 88  ASP B OD1 
3559 O OD2 . ASP B 87  ? 0.6414 0.5709 0.9061 -0.0379 0.2321  -0.0644 88  ASP B OD2 
3560 N N   . ASP B 88  ? 0.5250 0.3380 0.5603 -0.0610 0.2750  -0.0678 89  ASP B N   
3561 C CA  . ASP B 88  ? 0.6258 0.3953 0.6012 -0.0675 0.2878  -0.0701 89  ASP B CA  
3562 C C   . ASP B 88  ? 0.6070 0.3697 0.5320 -0.0683 0.2735  -0.0686 89  ASP B C   
3563 O O   . ASP B 88  ? 0.5717 0.3612 0.5047 -0.0642 0.2526  -0.0642 89  ASP B O   
3564 C CB  . ASP B 88  ? 0.5647 0.3104 0.5174 -0.0711 0.2977  -0.0686 89  ASP B CB  
3565 C CG  . ASP B 88  ? 0.6644 0.4071 0.6595 -0.0711 0.3148  -0.0718 89  ASP B CG  
3566 O OD1 . ASP B 88  ? 0.6221 0.3751 0.6579 -0.0694 0.3199  -0.0753 89  ASP B OD1 
3567 O OD2 . ASP B 88  ? 0.6710 0.4002 0.6592 -0.0727 0.3227  -0.0709 89  ASP B OD2 
3568 N N   . THR B 89  ? 0.6467 0.3717 0.5199 -0.0735 0.2799  -0.0713 90  THR B N   
3569 C CA  . THR B 89  ? 0.6470 0.3574 0.4657 -0.0747 0.2637  -0.0705 90  THR B CA  
3570 C C   . THR B 89  ? 0.7165 0.3906 0.4769 -0.0796 0.2622  -0.0670 90  THR B C   
3571 O O   . THR B 89  ? 0.7258 0.3797 0.4835 -0.0830 0.2789  -0.0668 90  THR B O   
3572 C CB  . THR B 89  ? 0.6528 0.3482 0.4564 -0.0765 0.2660  -0.0760 90  THR B CB  
3573 O OG1 . THR B 89  ? 0.6949 0.3553 0.4798 -0.0827 0.2861  -0.0784 90  THR B OG1 
3574 C CG2 . THR B 89  ? 0.6338 0.3654 0.4972 -0.0710 0.2661  -0.0787 90  THR B CG2 
3575 N N   . PRO B 90  ? 0.7197 0.3840 0.4343 -0.0800 0.2409  -0.0641 91  PRO B N   
3576 C CA  . PRO B 90  ? 0.7149 0.3486 0.3799 -0.0837 0.2352  -0.0589 91  PRO B CA  
3577 C C   . PRO B 90  ? 0.8545 0.4429 0.4805 -0.0899 0.2500  -0.0606 91  PRO B C   
3578 O O   . PRO B 90  ? 0.8545 0.4196 0.4575 -0.0926 0.2562  -0.0574 91  PRO B O   
3579 C CB  . PRO B 90  ? 0.7373 0.3708 0.3675 -0.0824 0.2049  -0.0559 91  PRO B CB  
3580 C CG  . PRO B 90  ? 0.7300 0.3849 0.3869 -0.0794 0.1945  -0.0595 91  PRO B CG  
3581 C CD  . PRO B 90  ? 0.6679 0.3553 0.3888 -0.0758 0.2114  -0.0619 91  PRO B CD  
3582 N N   . GLY B 91  ? 0.8110 0.3853 0.4283 -0.0924 0.2566  -0.0657 92  GLY B N   
3583 C CA  . GLY B 91  ? 0.9261 0.4550 0.5023 -0.0989 0.2706  -0.0672 92  GLY B CA  
3584 C C   . GLY B 91  ? 0.9138 0.4311 0.5123 -0.1014 0.2998  -0.0690 92  GLY B C   
3585 O O   . GLY B 91  ? 0.9746 0.4503 0.5354 -0.1071 0.3131  -0.0695 92  GLY B O   
3586 N N   . LYS B 92  ? 0.8645 0.4165 0.5246 -0.0974 0.3093  -0.0702 93  LYS B N   
3587 C CA  . LYS B 92  ? 0.8766 0.4193 0.5631 -0.0991 0.3339  -0.0720 93  LYS B CA  
3588 C C   . LYS B 92  ? 0.8599 0.3821 0.5179 -0.1004 0.3346  -0.0678 93  LYS B C   
3589 O O   . LYS B 92  ? 0.8969 0.3927 0.5522 -0.1037 0.3560  -0.0697 93  LYS B O   
3590 C CB  . LYS B 92  ? 0.8263 0.4133 0.5884 -0.0936 0.3380  -0.0739 93  LYS B CB  
3591 C CG  . LYS B 92  ? 0.7940 0.3777 0.5912 -0.0938 0.3579  -0.0755 93  LYS B CG  
3592 C CD  . LYS B 92  ? 0.8228 0.4444 0.6943 -0.0890 0.3609  -0.0784 93  LYS B CD  
3593 C CE  . LYS B 92  ? 0.8279 0.4471 0.7379 -0.0886 0.3780  -0.0804 93  LYS B CE  
3594 N NZ  . LYS B 92  ? 0.8916 0.5475 0.8739 -0.0834 0.3758  -0.0827 93  LYS B NZ  
3595 N N   . TYR B 93  ? 0.8493 0.3811 0.4852 -0.0979 0.3119  -0.0623 94  TYR B N   
3596 C CA  . TYR B 93  ? 0.8998 0.4146 0.5099 -0.0986 0.3101  -0.0576 94  TYR B CA  
3597 C C   . TYR B 93  ? 0.9352 0.4143 0.4758 -0.1018 0.2935  -0.0534 94  TYR B C   
3598 O O   . TYR B 93  ? 0.9541 0.3981 0.4596 -0.1050 0.3010  -0.0517 94  TYR B O   
3599 C CB  . TYR B 93  ? 0.8427 0.3990 0.4910 -0.0931 0.2976  -0.0536 94  TYR B CB  
3600 C CG  . TYR B 93  ? 0.8002 0.3912 0.5194 -0.0896 0.3110  -0.0575 94  TYR B CG  
3601 C CD1 . TYR B 93  ? 0.8060 0.3911 0.5519 -0.0900 0.3307  -0.0596 94  TYR B CD1 
3602 C CD2 . TYR B 93  ? 0.7544 0.3821 0.5144 -0.0858 0.3031  -0.0594 94  TYR B CD2 
3603 C CE1 . TYR B 93  ? 0.7853 0.4002 0.5973 -0.0865 0.3398  -0.0632 94  TYR B CE1 
3604 C CE2 . TYR B 93  ? 0.7172 0.3753 0.5433 -0.0823 0.3122  -0.0625 94  TYR B CE2 
3605 C CZ  . TYR B 93  ? 0.7201 0.3712 0.5720 -0.0827 0.3294  -0.0644 94  TYR B CZ  
3606 O OH  . TYR B 93  ? 0.7047 0.3835 0.6225 -0.0790 0.3354  -0.0675 94  TYR B OH  
3607 N N   . TRP B 94  ? 0.9324 0.4189 0.4535 -0.1008 0.2702  -0.0519 95  TRP B N   
3608 C CA  . TRP B 94  ? 0.9515 0.4046 0.4107 -0.1035 0.2507  -0.0483 95  TRP B CA  
3609 C C   . TRP B 94  ? 1.0418 0.4690 0.4766 -0.1078 0.2574  -0.0531 95  TRP B C   
3610 O O   . TRP B 94  ? 0.9767 0.4208 0.4198 -0.1063 0.2454  -0.0554 95  TRP B O   
3611 C CB  . TRP B 94  ? 0.9276 0.4057 0.3847 -0.0994 0.2181  -0.0433 95  TRP B CB  
3612 C CG  . TRP B 94  ? 0.9646 0.4121 0.3667 -0.1013 0.1942  -0.0383 95  TRP B CG  
3613 C CD1 . TRP B 94  ? 1.0308 0.4310 0.3835 -0.1062 0.1987  -0.0380 95  TRP B CD1 
3614 C CD2 . TRP B 94  ? 0.9249 0.3866 0.3189 -0.0981 0.1609  -0.0328 95  TRP B CD2 
3615 N NE1 . TRP B 94  ? 1.0772 0.4620 0.3926 -0.1061 0.1694  -0.0326 95  TRP B NE1 
3616 C CE2 . TRP B 94  ? 1.0018 0.4246 0.3441 -0.1011 0.1456  -0.0293 95  TRP B CE2 
3617 C CE3 . TRP B 94  ? 0.9132 0.4157 0.3398 -0.0932 0.1425  -0.0305 95  TRP B CE3 
3618 C CZ2 . TRP B 94  ? 1.0427 0.4684 0.3708 -0.0989 0.1118  -0.0235 95  TRP B CZ2 
3619 C CZ3 . TRP B 94  ? 0.9378 0.4420 0.3482 -0.0913 0.1099  -0.0248 95  TRP B CZ3 
3620 C CH2 . TRP B 94  ? 1.0121 0.4794 0.3766 -0.0940 0.0945  -0.0213 95  TRP B CH2 
3621 N N   . LYS B 95  ? 1.0084 0.3927 0.4122 -0.1132 0.2774  -0.0549 96  LYS B N   
3622 C CA  . LYS B 95  ? 1.0743 0.4346 0.4647 -0.1179 0.2931  -0.0604 96  LYS B CA  
3623 C C   . LYS B 95  ? 1.0417 0.3878 0.3912 -0.1193 0.2699  -0.0599 96  LYS B C   
3624 O O   . LYS B 95  ? 1.0448 0.3907 0.3991 -0.1210 0.2758  -0.0648 96  LYS B O   
3625 C CB  . LYS B 95  ? 1.1896 0.5027 0.5504 -0.1237 0.3191  -0.0618 96  LYS B CB  
3626 C CG  . LYS B 95  ? 1.1738 0.4985 0.5791 -0.1226 0.3442  -0.0635 96  LYS B CG  
3627 C CD  . LYS B 95  ? 1.1951 0.5586 0.6666 -0.1200 0.3569  -0.0685 96  LYS B CD  
3628 C CE  . LYS B 95  ? 1.2337 0.6073 0.7535 -0.1188 0.3808  -0.0708 96  LYS B CE  
3629 N NZ  . LYS B 95  ? 1.1628 0.5707 0.7482 -0.1165 0.3919  -0.0756 96  LYS B NZ  
3630 N N   . GLU B 96  ? 1.0567 0.3916 0.3689 -0.1185 0.2427  -0.0543 97  GLU B N   
3631 C CA  . GLU B 96  ? 1.0754 0.3991 0.3538 -0.1192 0.2167  -0.0537 97  GLU B CA  
3632 C C   . GLU B 96  ? 1.0810 0.4466 0.3974 -0.1149 0.2033  -0.0567 97  GLU B C   
3633 O O   . GLU B 96  ? 1.0342 0.3922 0.3300 -0.1156 0.1854  -0.0582 97  GLU B O   
3634 C CB  . GLU B 96  ? 1.0948 0.4041 0.3376 -0.1182 0.1882  -0.0464 97  GLU B CB  
3635 C CG  . GLU B 96  ? 1.1683 0.4232 0.3558 -0.1235 0.1959  -0.0443 97  GLU B CG  
3636 C CD  . GLU B 96  ? 1.2760 0.5223 0.4731 -0.1244 0.2233  -0.0440 97  GLU B CD  
3637 O OE1 . GLU B 96  ? 1.1967 0.4799 0.4379 -0.1200 0.2260  -0.0426 97  GLU B OE1 
3638 O OE2 . GLU B 96  ? 1.2576 0.4582 0.4169 -0.1297 0.2420  -0.0454 97  GLU B OE2 
3639 N N   . LEU B 97  ? 0.9894 0.3975 0.3611 -0.1105 0.2117  -0.0582 98  LEU B N   
3640 C CA  . LEU B 97  ? 0.9443 0.3919 0.3543 -0.1060 0.2012  -0.0616 98  LEU B CA  
3641 C C   . LEU B 97  ? 0.9863 0.4431 0.4287 -0.1069 0.2257  -0.0690 98  LEU B C   
3642 O O   . LEU B 97  ? 0.9247 0.4114 0.3985 -0.1032 0.2185  -0.0727 98  LEU B O   
3643 C CB  . LEU B 97  ? 0.8999 0.3892 0.3513 -0.1002 0.1930  -0.0586 98  LEU B CB  
3644 C CG  . LEU B 97  ? 0.9486 0.4352 0.3768 -0.0986 0.1675  -0.0509 98  LEU B CG  
3645 C CD1 . LEU B 97  ? 0.9444 0.4714 0.4150 -0.0935 0.1646  -0.0482 98  LEU B CD1 
3646 C CD2 . LEU B 97  ? 0.9026 0.3830 0.3047 -0.0983 0.1357  -0.0495 98  LEU B CD2 
3647 N N   . LYS B 98  ? 1.0139 0.4456 0.4517 -0.1115 0.2541  -0.0712 99  LYS B N   
3648 C CA  . LYS B 98  ? 1.0405 0.4803 0.5134 -0.1126 0.2782  -0.0776 99  LYS B CA  
3649 C C   . LYS B 98  ? 1.0296 0.4656 0.4893 -0.1135 0.2687  -0.0822 99  LYS B C   
3650 O O   . LYS B 98  ? 1.0328 0.4383 0.4408 -0.1167 0.2544  -0.0814 99  LYS B O   
3651 C CB  . LYS B 98  ? 1.1001 0.5038 0.5595 -0.1187 0.3082  -0.0788 99  LYS B CB  
3652 C CG  . LYS B 98  ? 1.1361 0.5539 0.6374 -0.1172 0.3273  -0.0779 99  LYS B CG  
3653 C CD  . LYS B 98  ? 1.1375 0.5906 0.7071 -0.1144 0.3426  -0.0824 99  LYS B CD  
3654 C CE  . LYS B 98  ? 1.1861 0.6209 0.7522 -0.1189 0.3587  -0.0879 99  LYS B CE  
3655 N NZ  . LYS B 98  ? 1.2475 0.7042 0.8785 -0.1180 0.3804  -0.0918 99  LYS B NZ  
3656 N N   . ASN B 99  ? 1.0345 0.5021 0.5433 -0.1103 0.2758  -0.0871 100 ASN B N   
3657 C CA  . ASN B 99  ? 1.0492 0.5169 0.5555 -0.1106 0.2705  -0.0927 100 ASN B CA  
3658 C C   . ASN B 99  ? 1.0659 0.5379 0.5466 -0.1081 0.2361  -0.0919 100 ASN B C   
3659 O O   . ASN B 99  ? 1.0205 0.4806 0.4824 -0.1097 0.2276  -0.0961 100 ASN B O   
3660 C CB  . ASN B 99  ? 1.1640 0.5891 0.6342 -0.1180 0.2892  -0.0959 100 ASN B CB  
3661 C CG  . ASN B 99  ? 1.2102 0.6311 0.7119 -0.1209 0.3236  -0.0976 100 ASN B CG  
3662 O OD1 . ASN B 99  ? 1.1955 0.6478 0.7506 -0.1171 0.3323  -0.0967 100 ASN B OD1 
3663 N ND2 . ASN B 99  ? 1.2838 0.6646 0.7534 -0.1280 0.3428  -0.1001 100 ASN B ND2 
3664 N N   . THR B 100 ? 0.9768 0.4649 0.4581 -0.1044 0.2155  -0.0867 101 THR B N   
3665 C CA  . THR B 100 ? 0.9077 0.4066 0.3785 -0.1015 0.1821  -0.0858 101 THR B CA  
3666 C C   . THR B 100 ? 0.8226 0.3665 0.3477 -0.0950 0.1763  -0.0883 101 THR B C   
3667 O O   . THR B 100 ? 0.8088 0.3759 0.3759 -0.0922 0.1948  -0.0886 101 THR B O   
3668 C CB  . THR B 100 ? 0.9327 0.4185 0.3688 -0.1018 0.1606  -0.0778 101 THR B CB  
3669 O OG1 . THR B 100 ? 0.8948 0.4066 0.3609 -0.0980 0.1643  -0.0739 101 THR B OG1 
3670 C CG2 . THR B 100 ? 0.9939 0.4332 0.3787 -0.1079 0.1698  -0.0750 101 THR B CG2 
3671 N N   . PRO B 101 ? 0.8463 0.4027 0.3743 -0.0926 0.1503  -0.0900 102 PRO B N   
3672 C CA  . PRO B 101 ? 0.7633 0.3612 0.3457 -0.0867 0.1452  -0.0918 102 PRO B CA  
3673 C C   . PRO B 101 ? 0.7149 0.3474 0.3341 -0.0815 0.1411  -0.0824 102 PRO B C   
3674 O O   . PRO B 101 ? 0.6605 0.3315 0.3379 -0.0762 0.1471  -0.0803 102 PRO B O   
3675 C CB  . PRO B 101 ? 0.7551 0.3591 0.3334 -0.0856 0.1128  -0.0907 102 PRO B CB  
3676 C CG  . PRO B 101 ? 0.8029 0.3649 0.3300 -0.0917 0.1134  -0.0958 102 PRO B CG  
3677 C CD  . PRO B 101 ? 0.8486 0.3833 0.3399 -0.0953 0.1273  -0.0908 102 PRO B CD  
3678 N N   . ILE B 102 ? 0.7909 0.4099 0.3781 -0.0830 0.1307  -0.0769 103 ILE B N   
3679 C CA  . ILE B 102 ? 0.6920 0.3427 0.3144 -0.0784 0.1282  -0.0688 103 ILE B CA  
3680 C C   . ILE B 102 ? 0.7123 0.3673 0.3597 -0.0785 0.1604  -0.0712 103 ILE B C   
3681 O O   . ILE B 102 ? 0.6732 0.3622 0.3660 -0.0738 0.1610  -0.0663 103 ILE B O   
3682 C CB  . ILE B 102 ? 0.7214 0.3544 0.3037 -0.0801 0.1111  -0.0625 103 ILE B CB  
3683 C CG1 . ILE B 102 ? 0.6788 0.3485 0.3014 -0.0747 0.1038  -0.0542 103 ILE B CG1 
3684 C CG2 . ILE B 102 ? 0.7650 0.3501 0.2911 -0.0867 0.1313  -0.0652 103 ILE B CG2 
3685 C CD1 . ILE B 102 ? 0.6249 0.3388 0.2978 -0.0682 0.0833  -0.0501 103 ILE B CD1 
3686 N N   . ASP B 103 ? 0.7292 0.3496 0.3495 -0.0838 0.1875  -0.0791 104 ASP B N   
3687 C CA  . ASP B 103 ? 0.7357 0.3603 0.3873 -0.0842 0.2184  -0.0809 104 ASP B CA  
3688 C C   . ASP B 103 ? 0.6830 0.3431 0.3981 -0.0793 0.2272  -0.0845 104 ASP B C   
3689 O O   . ASP B 103 ? 0.6852 0.3514 0.4347 -0.0793 0.2508  -0.0859 104 ASP B O   
3690 C CB  . ASP B 103 ? 0.7836 0.3686 0.4024 -0.0910 0.2364  -0.0820 104 ASP B CB  
3691 C CG  . ASP B 103 ? 0.8282 0.4084 0.4679 -0.0930 0.2626  -0.0805 104 ASP B CG  
3692 O OD1 . ASP B 103 ? 0.8098 0.4090 0.4721 -0.0901 0.2622  -0.0766 104 ASP B OD1 
3693 O OD2 . ASP B 103 ? 0.8803 0.4368 0.5147 -0.0978 0.2836  -0.0833 104 ASP B OD2 
3694 N N   . GLN B 104 ? 0.6330 0.3201 0.3724 -0.0749 0.2041  -0.0825 105 GLN B N   
3695 C CA  . GLN B 104 ? 0.6069 0.3335 0.4111 -0.0690 0.2050  -0.0819 105 GLN B CA  
3696 C C   . GLN B 104 ? 0.5629 0.3318 0.4110 -0.0626 0.1881  -0.0731 105 GLN B C   
3697 O O   . GLN B 104 ? 0.5168 0.3179 0.4178 -0.0575 0.1877  -0.0716 105 GLN B O   
3698 C CB  . GLN B 104 ? 0.6287 0.3599 0.4356 -0.0678 0.1910  -0.0844 105 GLN B CB  
3699 C CG  . GLN B 104 ? 0.7039 0.3958 0.4744 -0.0738 0.2086  -0.0944 105 GLN B CG  
3700 C CD  . GLN B 104 ? 0.7566 0.4425 0.5530 -0.0750 0.2428  -0.1007 105 GLN B CD  
3701 O OE1 . GLN B 104 ? 0.7199 0.3767 0.4886 -0.0810 0.2600  -0.1011 105 GLN B OE1 
3702 N NE2 . GLN B 104 ? 0.7712 0.4925 0.6306 -0.0694 0.2454  -0.0993 105 GLN B NE2 
3703 N N   . VAL B 105 ? 0.5598 0.3277 0.3858 -0.0628 0.1737  -0.0673 106 VAL B N   
3704 C CA  . VAL B 105 ? 0.5254 0.3294 0.3870 -0.0572 0.1581  -0.0595 106 VAL B CA  
3705 C C   . VAL B 105 ? 0.5502 0.3542 0.4257 -0.0581 0.1767  -0.0592 106 VAL B C   
3706 O O   . VAL B 105 ? 0.5789 0.3503 0.4166 -0.0635 0.1920  -0.0616 106 VAL B O   
3707 C CB  . VAL B 105 ? 0.5605 0.3639 0.3935 -0.0568 0.1312  -0.0535 106 VAL B CB  
3708 C CG1 . VAL B 105 ? 0.4504 0.2890 0.3180 -0.0513 0.1168  -0.0461 106 VAL B CG1 
3709 C CG2 . VAL B 105 ? 0.5138 0.3149 0.3345 -0.0565 0.1134  -0.0545 106 VAL B CG2 
3710 N N   . ASN B 106 ? 0.4953 0.3339 0.4238 -0.0531 0.1754  -0.0563 107 ASN B N   
3711 C CA  . ASN B 106 ? 0.4820 0.3209 0.4274 -0.0542 0.1921  -0.0564 107 ASN B CA  
3712 C C   . ASN B 106 ? 0.4704 0.3198 0.4089 -0.0527 0.1758  -0.0497 107 ASN B C   
3713 O O   . ASN B 106 ? 0.4680 0.3296 0.3975 -0.0500 0.1515  -0.0448 107 ASN B O   
3714 C CB  . ASN B 106 ? 0.4552 0.3206 0.4627 -0.0505 0.2024  -0.0581 107 ASN B CB  
3715 C CG  . ASN B 106 ? 0.4215 0.3270 0.4693 -0.0436 0.1788  -0.0522 107 ASN B CG  
3716 O OD1 . ASN B 106 ? 0.4262 0.3437 0.4667 -0.0415 0.1604  -0.0467 107 ASN B OD1 
3717 N ND2 . ASN B 106 ? 0.3655 0.2902 0.4563 -0.0399 0.1802  -0.0534 107 ASN B ND2 
3718 N N   . LEU B 107 ? 0.4315 0.2754 0.3765 -0.0547 0.1908  -0.0499 108 LEU B N   
3719 C CA  . LEU B 107 ? 0.4637 0.3108 0.3965 -0.0543 0.1791  -0.0443 108 LEU B CA  
3720 C C   . LEU B 107 ? 0.4207 0.3070 0.3903 -0.0480 0.1558  -0.0392 108 LEU B C   
3721 O O   . LEU B 107 ? 0.4460 0.3368 0.3991 -0.0467 0.1372  -0.0341 108 LEU B O   
3722 C CB  . LEU B 107 ? 0.4810 0.3155 0.4200 -0.0577 0.2022  -0.0460 108 LEU B CB  
3723 C CG  . LEU B 107 ? 0.5502 0.3420 0.4506 -0.0644 0.2296  -0.0512 108 LEU B CG  
3724 C CD1 . LEU B 107 ? 0.5766 0.3569 0.4853 -0.0676 0.2525  -0.0519 108 LEU B CD1 
3725 C CD2 . LEU B 107 ? 0.6140 0.3738 0.4479 -0.0678 0.2190  -0.0493 108 LEU B CD2 
3726 N N   . LEU B 108 ? 0.3754 0.2886 0.3944 -0.0440 0.1564  -0.0404 109 LEU B N   
3727 C CA  . LEU B 108 ? 0.3552 0.3019 0.4043 -0.0381 0.1345  -0.0356 109 LEU B CA  
3728 C C   . LEU B 108 ? 0.3417 0.2938 0.3716 -0.0357 0.1134  -0.0321 109 LEU B C   
3729 O O   . LEU B 108 ? 0.3197 0.2872 0.3505 -0.0326 0.0949  -0.0272 109 LEU B O   
3730 C CB  . LEU B 108 ? 0.3554 0.3259 0.4577 -0.0344 0.1380  -0.0374 109 LEU B CB  
3731 C CG  . LEU B 108 ? 0.3537 0.3558 0.4842 -0.0284 0.1158  -0.0327 109 LEU B CG  
3732 C CD1 . LEU B 108 ? 0.3332 0.3417 0.4629 -0.0282 0.1086  -0.0301 109 LEU B CD1 
3733 C CD2 . LEU B 108 ? 0.4109 0.4328 0.5909 -0.0248 0.1175  -0.0341 109 LEU B CD2 
3734 N N   . GLN B 109 ? 0.3453 0.2840 0.3592 -0.0372 0.1166  -0.0348 110 GLN B N   
3735 C CA  . GLN B 109 ? 0.3320 0.2748 0.3309 -0.0352 0.0975  -0.0320 110 GLN B CA  
3736 C C   . GLN B 109 ? 0.3127 0.2386 0.2703 -0.0377 0.0860  -0.0290 110 GLN B C   
3737 O O   . GLN B 109 ? 0.3267 0.2649 0.2834 -0.0348 0.0663  -0.0246 110 GLN B O   
3738 C CB  . GLN B 109 ? 0.3143 0.2455 0.3079 -0.0366 0.1047  -0.0365 110 GLN B CB  
3739 C CG  . GLN B 109 ? 0.2863 0.2381 0.3260 -0.0330 0.1116  -0.0379 110 GLN B CG  
3740 C CD  . GLN B 109 ? 0.3826 0.3199 0.4208 -0.0351 0.1252  -0.0437 110 GLN B CD  
3741 O OE1 . GLN B 109 ? 0.3790 0.2862 0.3835 -0.0405 0.1387  -0.0486 110 GLN B OE1 
3742 N NE2 . GLN B 109 ? 0.3278 0.2847 0.4011 -0.0309 0.1220  -0.0430 110 GLN B NE2 
3743 N N   . LEU B 110 ? 0.3397 0.2358 0.2629 -0.0430 0.0981  -0.0312 111 LEU B N   
3744 C CA  . LEU B 110 ? 0.4332 0.3126 0.3186 -0.0451 0.0859  -0.0275 111 LEU B CA  
3745 C C   . LEU B 110 ? 0.3740 0.2748 0.2782 -0.0418 0.0751  -0.0222 111 LEU B C   
3746 O O   . LEU B 110 ? 0.3844 0.2901 0.2795 -0.0401 0.0560  -0.0177 111 LEU B O   
3747 C CB  . LEU B 110 ? 0.4364 0.2772 0.2796 -0.0515 0.1028  -0.0304 111 LEU B CB  
3748 C CG  . LEU B 110 ? 0.4528 0.2643 0.2659 -0.0558 0.1138  -0.0363 111 LEU B CG  
3749 C CD1 . LEU B 110 ? 0.5373 0.3116 0.3143 -0.0619 0.1368  -0.0394 111 LEU B CD1 
3750 C CD2 . LEU B 110 ? 0.4508 0.2503 0.2324 -0.0565 0.0921  -0.0350 111 LEU B CD2 
3751 N N   . ALA B 111 ? 0.3525 0.2662 0.2855 -0.0408 0.0870  -0.0230 112 ALA B N   
3752 C CA  . ALA B 111 ? 0.3496 0.2802 0.2980 -0.0383 0.0785  -0.0190 112 ALA B CA  
3753 C C   . ALA B 111 ? 0.3424 0.3034 0.3174 -0.0326 0.0595  -0.0156 112 ALA B C   
3754 O O   . ALA B 111 ? 0.3131 0.2843 0.2911 -0.0306 0.0482  -0.0119 112 ALA B O   
3755 C CB  . ALA B 111 ? 0.3444 0.2809 0.3202 -0.0390 0.0956  -0.0216 112 ALA B CB  
3756 N N   . THR B 112 ? 0.2917 0.2659 0.2856 -0.0299 0.0570  -0.0168 113 THR B N   
3757 C CA  . THR B 112 ? 0.2670 0.2676 0.2847 -0.0245 0.0415  -0.0135 113 THR B CA  
3758 C C   . THR B 112 ? 0.2706 0.2691 0.2764 -0.0236 0.0304  -0.0121 113 THR B C   
3759 O O   . THR B 112 ? 0.2335 0.2509 0.2597 -0.0194 0.0217  -0.0100 113 THR B O   
3760 C CB  . THR B 112 ? 0.2931 0.3137 0.3492 -0.0213 0.0467  -0.0151 113 THR B CB  
3761 O OG1 . THR B 112 ? 0.2539 0.2669 0.3143 -0.0226 0.0578  -0.0188 113 THR B OG1 
3762 C CG2 . THR B 112 ? 0.2412 0.2652 0.3142 -0.0222 0.0557  -0.0167 113 THR B CG2 
3763 N N   . TYR B 113 ? 0.2695 0.2436 0.2419 -0.0276 0.0304  -0.0133 114 TYR B N   
3764 C CA  . TYR B 113 ? 0.2897 0.2591 0.2473 -0.0274 0.0155  -0.0114 114 TYR B CA  
3765 C C   . TYR B 113 ? 0.2816 0.2562 0.2513 -0.0261 0.0160  -0.0135 114 TYR B C   
3766 O O   . TYR B 113 ? 0.2718 0.2542 0.2465 -0.0240 0.0029  -0.0111 114 TYR B O   
3767 C CB  . TYR B 113 ? 0.2811 0.2681 0.2505 -0.0235 -0.0008 -0.0060 114 TYR B CB  
3768 C CG  . TYR B 113 ? 0.2525 0.2417 0.2208 -0.0235 -0.0012 -0.0037 114 TYR B CG  
3769 C CD1 . TYR B 113 ? 0.3113 0.2777 0.2500 -0.0275 -0.0003 -0.0034 114 TYR B CD1 
3770 C CD2 . TYR B 113 ? 0.2371 0.2495 0.2323 -0.0195 -0.0029 -0.0018 114 TYR B CD2 
3771 C CE1 . TYR B 113 ? 0.3093 0.2776 0.2486 -0.0273 -0.0003 -0.0010 114 TYR B CE1 
3772 C CE2 . TYR B 113 ? 0.2751 0.2892 0.2703 -0.0195 -0.0032 -0.0003 114 TYR B CE2 
3773 C CZ  . TYR B 113 ? 0.2998 0.2928 0.2688 -0.0234 -0.0016 0.0001  114 TYR B CZ  
3774 O OH  . TYR B 113 ? 0.3805 0.3753 0.3513 -0.0234 -0.0015 0.0018  114 TYR B OH  
3775 N N   . THR B 114 ? 0.2815 0.2515 0.2582 -0.0274 0.0315  -0.0180 115 THR B N   
3776 C CA  . THR B 114 ? 0.2601 0.2366 0.2523 -0.0258 0.0324  -0.0198 115 THR B CA  
3777 C C   . THR B 114 ? 0.3322 0.2821 0.2994 -0.0306 0.0420  -0.0257 115 THR B C   
3778 O O   . THR B 114 ? 0.3142 0.2666 0.2962 -0.0300 0.0492  -0.0287 115 THR B O   
3779 C CB  . THR B 114 ? 0.2878 0.2857 0.3181 -0.0219 0.0402  -0.0197 115 THR B CB  
3780 O OG1 . THR B 114 ? 0.3014 0.2907 0.3353 -0.0245 0.0578  -0.0237 115 THR B OG1 
3781 C CG2 . THR B 114 ? 0.2674 0.2900 0.3195 -0.0170 0.0288  -0.0142 115 THR B CG2 
3782 N N   . SER B 115 ? 0.3007 0.2234 0.2283 -0.0355 0.0409  -0.0273 116 SER B N   
3783 C CA  . SER B 115 ? 0.3558 0.2492 0.2533 -0.0404 0.0486  -0.0333 116 SER B CA  
3784 C C   . SER B 115 ? 0.3658 0.2630 0.2691 -0.0393 0.0374  -0.0343 116 SER B C   
3785 O O   . SER B 115 ? 0.3656 0.2460 0.2577 -0.0423 0.0463  -0.0401 116 SER B O   
3786 C CB  . SER B 115 ? 0.3976 0.2589 0.2468 -0.0456 0.0449  -0.0337 116 SER B CB  
3787 O OG  . SER B 115 ? 0.3995 0.2616 0.2388 -0.0448 0.0213  -0.0301 116 SER B OG  
3788 N N   . GLY B 116 ? 0.3269 0.2438 0.2466 -0.0355 0.0188  -0.0290 117 GLY B N   
3789 C CA  . GLY B 116 ? 0.3364 0.2581 0.2654 -0.0344 0.0080  -0.0293 117 GLY B CA  
3790 C C   . GLY B 116 ? 0.3638 0.2652 0.2632 -0.0378 -0.0090 -0.0300 117 GLY B C   
3791 O O   . GLY B 116 ? 0.3987 0.3055 0.3095 -0.0368 -0.0204 -0.0299 117 GLY B O   
3792 N N   . ASN B 117 ? 0.3592 0.2362 0.2215 -0.0418 -0.0116 -0.0305 118 ASN B N   
3793 C CA  . ASN B 117 ? 0.3958 0.2527 0.2307 -0.0448 -0.0315 -0.0305 118 ASN B CA  
3794 C C   . ASN B 117 ? 0.4280 0.2670 0.2316 -0.0472 -0.0376 -0.0275 118 ASN B C   
3795 O O   . ASN B 117 ? 0.4627 0.2672 0.2221 -0.0524 -0.0407 -0.0305 118 ASN B O   
3796 C CB  . ASN B 117 ? 0.4175 0.2457 0.2239 -0.0498 -0.0294 -0.0380 118 ASN B CB  
3797 C CG  . ASN B 117 ? 0.4398 0.2512 0.2268 -0.0523 -0.0540 -0.0383 118 ASN B CG  
3798 O OD1 . ASN B 117 ? 0.4531 0.2829 0.2639 -0.0491 -0.0717 -0.0332 118 ASN B OD1 
3799 N ND2 . ASN B 117 ? 0.5154 0.2906 0.2596 -0.0582 -0.0551 -0.0447 118 ASN B ND2 
3800 N N   . LEU B 118 ? 0.4169 0.2770 0.2410 -0.0435 -0.0394 -0.0216 119 LEU B N   
3801 C CA  . LEU B 118 ? 0.4536 0.3000 0.2538 -0.0450 -0.0472 -0.0176 119 LEU B CA  
3802 C C   . LEU B 118 ? 0.4346 0.3080 0.2669 -0.0401 -0.0622 -0.0111 119 LEU B C   
3803 O O   . LEU B 118 ? 0.3858 0.2885 0.2535 -0.0356 -0.0553 -0.0090 119 LEU B O   
3804 C CB  . LEU B 118 ? 0.4342 0.2728 0.2217 -0.0465 -0.0270 -0.0182 119 LEU B CB  
3805 C CG  . LEU B 118 ? 0.4812 0.2852 0.2294 -0.0523 -0.0104 -0.0245 119 LEU B CG  
3806 C CD1 . LEU B 118 ? 0.4817 0.2826 0.2285 -0.0533 0.0131  -0.0253 119 LEU B CD1 
3807 C CD2 . LEU B 118 ? 0.5520 0.3168 0.2478 -0.0574 -0.0244 -0.0249 119 LEU B CD2 
3808 N N   . ALA B 119 ? 0.4425 0.3048 0.2628 -0.0410 -0.0830 -0.0082 120 ALA B N   
3809 C CA  . ALA B 119 ? 0.4299 0.3142 0.2810 -0.0368 -0.0982 -0.0025 120 ALA B CA  
3810 C C   . ALA B 119 ? 0.4380 0.3249 0.2866 -0.0357 -0.0970 0.0021  120 ALA B C   
3811 O O   . ALA B 119 ? 0.4515 0.3249 0.2768 -0.0380 -0.0840 0.0012  120 ALA B O   
3812 C CB  . ALA B 119 ? 0.4882 0.3589 0.3328 -0.0384 -0.1221 -0.0019 120 ALA B CB  
3813 N N   . LEU B 120 ? 0.4202 0.3240 0.2946 -0.0321 -0.1098 0.0071  121 LEU B N   
3814 C CA  . LEU B 120 ? 0.4197 0.3291 0.2972 -0.0305 -0.1085 0.0114  121 LEU B CA  
3815 C C   . LEU B 120 ? 0.4553 0.3326 0.2909 -0.0348 -0.1137 0.0128  121 LEU B C   
3816 O O   . LEU B 120 ? 0.4724 0.3453 0.2962 -0.0356 -0.1018 0.0137  121 LEU B O   
3817 C CB  . LEU B 120 ? 0.4249 0.3548 0.3371 -0.0263 -0.1215 0.0159  121 LEU B CB  
3818 C CG  . LEU B 120 ? 0.4876 0.4233 0.4061 -0.0245 -0.1220 0.0202  121 LEU B CG  
3819 C CD1 . LEU B 120 ? 0.4039 0.3566 0.3327 -0.0226 -0.1025 0.0190  121 LEU B CD1 
3820 C CD2 . LEU B 120 ? 0.4906 0.4416 0.4421 -0.0208 -0.1356 0.0240  121 LEU B CD2 
3821 N N   . GLN B 121 ? 0.5038 0.3570 0.3159 -0.0378 -0.1317 0.0130  122 GLN B N   
3822 C CA  . GLN B 121 ? 0.5571 0.3751 0.3238 -0.0420 -0.1390 0.0149  122 GLN B CA  
3823 C C   . GLN B 121 ? 0.6072 0.3927 0.3319 -0.0473 -0.1401 0.0099  122 GLN B C   
3824 O O   . GLN B 121 ? 0.5717 0.3628 0.3070 -0.0474 -0.1413 0.0055  122 GLN B O   
3825 C CB  . GLN B 121 ? 0.5573 0.3733 0.3363 -0.0400 -0.1596 0.0205  122 GLN B CB  
3826 C CG  . GLN B 121 ? 0.5338 0.3805 0.3565 -0.0348 -0.1608 0.0247  122 GLN B CG  
3827 C CD  . GLN B 121 ? 0.5412 0.3881 0.3528 -0.0350 -0.1509 0.0277  122 GLN B CD  
3828 O OE1 . GLN B 121 ? 0.5722 0.3947 0.3454 -0.0387 -0.1415 0.0272  122 GLN B OE1 
3829 N NE2 . GLN B 121 ? 0.5409 0.4162 0.3909 -0.0305 -0.1475 0.0300  122 GLN B NE2 
3830 N N   . PHE B 122 ? 0.6183 0.3692 0.2965 -0.0514 -0.1375 0.0107  123 PHE B N   
3831 C CA  . PHE B 122 ? 0.7291 0.4470 0.3709 -0.0555 -0.1396 0.0071  123 PHE B CA  
3832 C C   . PHE B 122 ? 0.7625 0.4823 0.4242 -0.0535 -0.1627 0.0087  123 PHE B C   
3833 O O   . PHE B 122 ? 0.6909 0.4316 0.3893 -0.0493 -0.1752 0.0134  123 PHE B O   
3834 C CB  . PHE B 122 ? 0.7439 0.4264 0.3408 -0.0590 -0.1329 0.0094  123 PHE B CB  
3835 C CG  . PHE B 122 ? 0.7594 0.4289 0.3279 -0.0624 -0.1056 0.0060  123 PHE B CG  
3836 C CD1 . PHE B 122 ? 0.7454 0.3935 0.2853 -0.0666 -0.0900 -0.0010 123 PHE B CD1 
3837 C CD2 . PHE B 122 ? 0.7422 0.4202 0.3149 -0.0615 -0.0938 0.0095  123 PHE B CD2 
3838 C CE1 . PHE B 122 ? 0.7326 0.3689 0.2523 -0.0696 -0.0612 -0.0046 123 PHE B CE1 
3839 C CE2 . PHE B 122 ? 0.7142 0.3822 0.2693 -0.0644 -0.0654 0.0063  123 PHE B CE2 
3840 C CZ  . PHE B 122 ? 0.7709 0.4175 0.2993 -0.0685 -0.0486 -0.0008 123 PHE B CZ  
3841 N N   . PRO B 123 ? 0.7886 0.4859 0.4274 -0.0565 -0.1675 0.0047  124 PRO B N   
3842 C CA  . PRO B 123 ? 0.8451 0.5360 0.4952 -0.0554 -0.1900 0.0067  124 PRO B CA  
3843 C C   . PRO B 123 ? 0.8686 0.5420 0.5065 -0.0553 -0.2011 0.0129  124 PRO B C   
3844 O O   . PRO B 123 ? 0.8503 0.5033 0.4542 -0.0578 -0.1914 0.0145  124 PRO B O   
3845 C CB  . PRO B 123 ? 0.8905 0.5527 0.5052 -0.0597 -0.1896 0.0010  124 PRO B CB  
3846 C CG  . PRO B 123 ? 0.8431 0.5111 0.4489 -0.0617 -0.1674 -0.0054 124 PRO B CG  
3847 C CD  . PRO B 123 ? 0.8156 0.4936 0.4214 -0.0609 -0.1519 -0.0026 124 PRO B CD  
3848 N N   . ASP B 124 ? 0.8861 0.5671 0.5537 -0.0526 -0.2209 0.0162  125 ASP B N   
3849 C CA  . ASP B 124 ? 0.9099 0.5762 0.5718 -0.0524 -0.2333 0.0218  125 ASP B CA  
3850 C C   . ASP B 124 ? 0.9393 0.5601 0.5441 -0.0574 -0.2366 0.0218  125 ASP B C   
3851 O O   . ASP B 124 ? 0.9743 0.5782 0.5595 -0.0584 -0.2382 0.0259  125 ASP B O   
3852 C CB  . ASP B 124 ? 0.9342 0.6129 0.6375 -0.0492 -0.2535 0.0241  125 ASP B CB  
3853 C CG  . ASP B 124 ? 1.0089 0.7284 0.7662 -0.0448 -0.2488 0.0230  125 ASP B CG  
3854 O OD1 . ASP B 124 ? 1.0297 0.7575 0.7922 -0.0450 -0.2441 0.0184  125 ASP B OD1 
3855 O OD2 . ASP B 124 ? 1.0043 0.7465 0.7975 -0.0413 -0.2487 0.0265  125 ASP B OD2 
3856 N N   . GLU B 125 ? 0.9418 0.5412 0.5186 -0.0605 -0.2370 0.0172  126 GLU B N   
3857 C CA  . GLU B 125 ? 1.0279 0.5811 0.5481 -0.0654 -0.2397 0.0170  126 GLU B CA  
3858 C C   . GLU B 125 ? 1.0176 0.5526 0.4963 -0.0689 -0.2153 0.0155  126 GLU B C   
3859 O O   . GLU B 125 ? 1.0576 0.5524 0.4873 -0.0731 -0.2140 0.0158  126 GLU B O   
3860 C CB  . GLU B 125 ? 1.0506 0.5859 0.5547 -0.0677 -0.2481 0.0122  126 GLU B CB  
3861 C CG  . GLU B 125 ? 1.0912 0.6392 0.5958 -0.0687 -0.2295 0.0054  126 GLU B CG  
3862 C CD  . GLU B 125 ? 1.0623 0.6493 0.6213 -0.0646 -0.2357 0.0034  126 GLU B CD  
3863 O OE1 . GLU B 125 ? 1.1086 0.6974 0.6662 -0.0659 -0.2306 -0.0026 126 GLU B OE1 
3864 O OE2 . GLU B 125 ? 1.0344 0.6491 0.6379 -0.0602 -0.2446 0.0077  126 GLU B OE2 
3865 N N   . VAL B 126 ? 0.9853 0.5473 0.4826 -0.0673 -0.1956 0.0141  127 VAL B N   
3866 C CA  . VAL B 126 ? 1.0084 0.5556 0.4723 -0.0705 -0.1696 0.0121  127 VAL B CA  
3867 C C   . VAL B 126 ? 0.9973 0.5436 0.4596 -0.0696 -0.1671 0.0179  127 VAL B C   
3868 O O   . VAL B 126 ? 0.9429 0.5220 0.4419 -0.0658 -0.1648 0.0205  127 VAL B O   
3869 C CB  . VAL B 126 ? 0.9043 0.4789 0.3888 -0.0696 -0.1499 0.0070  127 VAL B CB  
3870 C CG1 . VAL B 126 ? 0.9579 0.5185 0.4140 -0.0727 -0.1212 0.0050  127 VAL B CG1 
3871 C CG2 . VAL B 126 ? 0.9384 0.5111 0.4221 -0.0710 -0.1522 0.0007  127 VAL B CG2 
3872 N N   . LYS B 127 ? 1.0347 0.5420 0.4533 -0.0732 -0.1674 0.0201  128 LYS B N   
3873 C CA  . LYS B 127 ? 1.0192 0.5217 0.4332 -0.0726 -0.1668 0.0256  128 LYS B CA  
3874 C C   . LYS B 127 ? 1.0435 0.5138 0.4113 -0.0770 -0.1430 0.0246  128 LYS B C   
3875 O O   . LYS B 127 ? 1.0353 0.5186 0.4114 -0.0762 -0.1246 0.0256  128 LYS B O   
3876 C CB  . LYS B 127 ? 1.0515 0.5382 0.4630 -0.0721 -0.1943 0.0304  128 LYS B CB  
3877 C CG  . LYS B 127 ? 1.1057 0.6239 0.5683 -0.0677 -0.2163 0.0317  128 LYS B CG  
3878 C CD  . LYS B 127 ? 1.1557 0.6529 0.6134 -0.0681 -0.2433 0.0354  128 LYS B CD  
3879 C CE  . LYS B 127 ? 1.1231 0.6536 0.6383 -0.0635 -0.2618 0.0368  128 LYS B CE  
3880 N NZ  . LYS B 127 ? 1.1168 0.6847 0.6753 -0.0593 -0.2552 0.0397  128 LYS B NZ  
3881 N N   . THR B 128 ? 1.0721 0.4997 0.3922 -0.0816 -0.1423 0.0226  129 THR B N   
3882 C CA  . THR B 128 ? 1.1317 0.5229 0.4055 -0.0860 -0.1201 0.0217  129 THR B CA  
3883 C C   . THR B 128 ? 1.1112 0.5111 0.3869 -0.0875 -0.0878 0.0160  129 THR B C   
3884 O O   . THR B 128 ? 1.1256 0.5552 0.4317 -0.0856 -0.0842 0.0123  129 THR B O   
3885 C CB  . THR B 128 ? 1.1867 0.5285 0.4085 -0.0907 -0.1286 0.0207  129 THR B CB  
3886 O OG1 . THR B 128 ? 1.2003 0.5333 0.4087 -0.0933 -0.1174 0.0143  129 THR B OG1 
3887 C CG2 . THR B 128 ? 1.2039 0.5433 0.4341 -0.0889 -0.1638 0.0247  129 THR B CG2 
3888 N N   . ASP B 129 ? 1.1355 0.5079 0.3791 -0.0910 -0.0635 0.0151  130 ASP B N   
3889 C CA  . ASP B 129 ? 1.1725 0.5485 0.4182 -0.0929 -0.0304 0.0093  130 ASP B CA  
3890 C C   . ASP B 129 ? 1.1666 0.5276 0.3955 -0.0960 -0.0250 0.0029  130 ASP B C   
3891 O O   . ASP B 129 ? 1.1308 0.5159 0.3852 -0.0952 -0.0113 -0.0020 130 ASP B O   
3892 C CB  . ASP B 129 ? 1.1514 0.4978 0.3678 -0.0961 -0.0053 0.0094  130 ASP B CB  
3893 C CG  . ASP B 129 ? 1.2022 0.5638 0.4356 -0.0932 -0.0078 0.0154  130 ASP B CG  
3894 O OD1 . ASP B 129 ? 1.1538 0.5577 0.4318 -0.0890 -0.0101 0.0170  130 ASP B OD1 
3895 O OD2 . ASP B 129 ? 1.2586 0.5884 0.4593 -0.0952 -0.0075 0.0186  130 ASP B OD2 
3896 N N   . GLN B 130 ? 1.2115 0.5310 0.3963 -0.0996 -0.0352 0.0029  131 GLN B N   
3897 C CA  . GLN B 130 ? 1.1869 0.4896 0.3531 -0.1028 -0.0309 -0.0029 131 GLN B CA  
3898 C C   . GLN B 130 ? 1.1612 0.4995 0.3648 -0.0992 -0.0502 -0.0045 131 GLN B C   
3899 O O   . GLN B 130 ? 1.1489 0.4938 0.3588 -0.1003 -0.0386 -0.0106 131 GLN B O   
3900 C CB  . GLN B 130 ? 1.3400 0.5902 0.4502 -0.1073 -0.0417 -0.0019 131 GLN B CB  
3901 C CG  . GLN B 130 ? 1.4083 0.6155 0.4743 -0.1123 -0.0143 -0.0032 131 GLN B CG  
3902 C CD  . GLN B 130 ? 1.3859 0.5969 0.4598 -0.1146 0.0219  -0.0100 131 GLN B CD  
3903 O OE1 . GLN B 130 ? 1.3187 0.5176 0.3801 -0.1174 0.0285  -0.0152 131 GLN B OE1 
3904 N NE2 . GLN B 130 ? 1.3110 0.5395 0.4086 -0.1133 0.0454  -0.0101 131 GLN B NE2 
3905 N N   . GLN B 131 ? 1.1523 0.5139 0.3832 -0.0949 -0.0786 0.0005  132 GLN B N   
3906 C CA  . GLN B 131 ? 1.1306 0.5279 0.4021 -0.0912 -0.0956 -0.0010 132 GLN B CA  
3907 C C   . GLN B 131 ? 1.0575 0.4952 0.3693 -0.0886 -0.0770 -0.0045 132 GLN B C   
3908 O O   . GLN B 131 ? 0.9939 0.4506 0.3261 -0.0876 -0.0773 -0.0094 132 GLN B O   
3909 C CB  . GLN B 131 ? 1.0948 0.5081 0.3916 -0.0871 -0.1275 0.0053  132 GLN B CB  
3910 C CG  . GLN B 131 ? 1.1289 0.5054 0.3925 -0.0894 -0.1509 0.0076  132 GLN B CG  
3911 C CD  . GLN B 131 ? 1.1666 0.5581 0.4588 -0.0855 -0.1801 0.0138  132 GLN B CD  
3912 O OE1 . GLN B 131 ? 1.1316 0.5488 0.4535 -0.0822 -0.1797 0.0177  132 GLN B OE1 
3913 N NE2 . GLN B 131 ? 1.1845 0.5599 0.4698 -0.0859 -0.2052 0.0145  132 GLN B NE2 
3914 N N   . VAL B 132 ? 1.0468 0.4975 0.3706 -0.0874 -0.0611 -0.0022 133 VAL B N   
3915 C CA  . VAL B 132 ? 1.0105 0.4954 0.3688 -0.0854 -0.0414 -0.0058 133 VAL B CA  
3916 C C   . VAL B 132 ? 1.0146 0.4864 0.3592 -0.0890 -0.0154 -0.0137 133 VAL B C   
3917 O O   . VAL B 132 ? 0.9387 0.4353 0.3101 -0.0877 -0.0101 -0.0189 133 VAL B O   
3918 C CB  . VAL B 132 ? 1.0004 0.4953 0.3690 -0.0842 -0.0270 -0.0020 133 VAL B CB  
3919 C CG1 . VAL B 132 ? 0.8705 0.3930 0.2685 -0.0832 -0.0019 -0.0067 133 VAL B CG1 
3920 C CG2 . VAL B 132 ? 1.0055 0.5223 0.3987 -0.0798 -0.0517 0.0052  133 VAL B CG2 
3921 N N   . LEU B 133 ? 1.0275 0.4593 0.3313 -0.0938 0.0019  -0.0150 134 LEU B N   
3922 C CA  . LEU B 133 ? 1.0704 0.4874 0.3626 -0.0976 0.0289  -0.0224 134 LEU B CA  
3923 C C   . LEU B 133 ? 1.0215 0.4366 0.3101 -0.0983 0.0163  -0.0270 134 LEU B C   
3924 O O   . LEU B 133 ? 0.9968 0.4269 0.3047 -0.0984 0.0318  -0.0337 134 LEU B O   
3925 C CB  . LEU B 133 ? 1.1036 0.4741 0.3507 -0.1028 0.0476  -0.0223 134 LEU B CB  
3926 C CG  . LEU B 133 ? 1.1216 0.4701 0.3538 -0.1074 0.0777  -0.0295 134 LEU B CG  
3927 C CD1 . LEU B 133 ? 1.0565 0.4404 0.3355 -0.1054 0.1019  -0.0343 134 LEU B CD1 
3928 C CD2 . LEU B 133 ? 1.1953 0.4984 0.3857 -0.1122 0.0963  -0.0285 134 LEU B CD2 
3929 N N   . THR B 134 ? 1.0256 0.4230 0.2922 -0.0987 -0.0117 -0.0239 135 THR B N   
3930 C CA  . THR B 134 ? 1.0514 0.4477 0.3167 -0.0991 -0.0259 -0.0282 135 THR B CA  
3931 C C   . THR B 134 ? 0.9666 0.4099 0.2833 -0.0944 -0.0350 -0.0306 135 THR B C   
3932 O O   . THR B 134 ? 0.9583 0.4095 0.2853 -0.0950 -0.0285 -0.0375 135 THR B O   
3933 C CB  . THR B 134 ? 1.0737 0.4448 0.3121 -0.0998 -0.0567 -0.0237 135 THR B CB  
3934 O OG1 . THR B 134 ? 1.1364 0.4572 0.3199 -0.1052 -0.0472 -0.0235 135 THR B OG1 
3935 C CG2 . THR B 134 ? 1.0341 0.4144 0.2847 -0.0989 -0.0765 -0.0274 135 THR B CG2 
3936 N N   . PHE B 135 ? 0.9538 0.4276 0.3032 -0.0898 -0.0498 -0.0252 136 PHE B N   
3937 C CA  . PHE B 135 ? 0.8695 0.3870 0.2677 -0.0854 -0.0573 -0.0271 136 PHE B CA  
3938 C C   . PHE B 135 ? 0.8759 0.4083 0.2904 -0.0859 -0.0285 -0.0346 136 PHE B C   
3939 O O   . PHE B 135 ? 0.8527 0.4037 0.2907 -0.0849 -0.0302 -0.0404 136 PHE B O   
3940 C CB  . PHE B 135 ? 0.8647 0.4096 0.2926 -0.0809 -0.0710 -0.0198 136 PHE B CB  
3941 C CG  . PHE B 135 ? 0.8417 0.4303 0.3188 -0.0766 -0.0759 -0.0213 136 PHE B CG  
3942 C CD1 . PHE B 135 ? 0.8222 0.4292 0.3271 -0.0738 -0.1002 -0.0209 136 PHE B CD1 
3943 C CD2 . PHE B 135 ? 0.8010 0.4113 0.2976 -0.0754 -0.0559 -0.0229 136 PHE B CD2 
3944 C CE1 . PHE B 135 ? 0.7850 0.4303 0.3350 -0.0702 -0.1041 -0.0220 136 PHE B CE1 
3945 C CE2 . PHE B 135 ? 0.7116 0.3623 0.2561 -0.0711 -0.0604 -0.0236 136 PHE B CE2 
3946 C CZ  . PHE B 135 ? 0.7128 0.3798 0.2820 -0.0688 -0.0846 -0.0231 136 PHE B CZ  
3947 N N   . PHE B 136 ? 0.8531 0.3775 0.2588 -0.0876 -0.0013 -0.0349 137 PHE B N   
3948 C CA  . PHE B 136 ? 0.8334 0.3740 0.2622 -0.0876 0.0270  -0.0420 137 PHE B CA  
3949 C C   . PHE B 136 ? 0.8465 0.3643 0.2574 -0.0916 0.0448  -0.0495 137 PHE B C   
3950 O O   . PHE B 136 ? 0.8015 0.3371 0.2394 -0.0907 0.0591  -0.0565 137 PHE B O   
3951 C CB  . PHE B 136 ? 0.8189 0.3629 0.2542 -0.0875 0.0506  -0.0397 137 PHE B CB  
3952 C CG  . PHE B 136 ? 0.8052 0.3834 0.2725 -0.0830 0.0403  -0.0350 137 PHE B CG  
3953 C CD1 . PHE B 136 ? 0.7362 0.3581 0.2579 -0.0779 0.0365  -0.0362 137 PHE B CD1 
3954 C CD2 . PHE B 136 ? 0.8145 0.3879 0.2727 -0.0823 0.0339  -0.0271 137 PHE B CD2 
3955 C CE1 . PHE B 136 ? 0.6888 0.3493 0.2550 -0.0723 0.0265  -0.0294 137 PHE B CE1 
3956 C CE2 . PHE B 136 ? 0.7771 0.3835 0.2684 -0.0780 0.0246  -0.0222 137 PHE B CE2 
3957 C CZ  . PHE B 136 ? 0.6706 0.3235 0.2220 -0.0724 0.0208  -0.0228 137 PHE B CZ  
3958 N N   . LYS B 137 ? 0.8759 0.3537 0.2425 -0.0959 0.0446  -0.0483 138 LYS B N   
3959 C CA  . LYS B 137 ? 0.9093 0.3645 0.2573 -0.0999 0.0591  -0.0553 138 LYS B CA  
3960 C C   . LYS B 137 ? 0.9208 0.3890 0.2818 -0.0985 0.0392  -0.0598 138 LYS B C   
3961 O O   . LYS B 137 ? 0.8964 0.3640 0.2643 -0.0999 0.0541  -0.0674 138 LYS B O   
3962 C CB  . LYS B 137 ? 0.9787 0.3852 0.2722 -0.1051 0.0606  -0.0528 138 LYS B CB  
3963 C CG  . LYS B 137 ? 1.0724 0.4572 0.3494 -0.1081 0.0879  -0.0509 138 LYS B CG  
3964 C CD  . LYS B 137 ? 1.1529 0.4847 0.3721 -0.1139 0.0897  -0.0497 138 LYS B CD  
3965 C CE  . LYS B 137 ? 1.1642 0.4707 0.3660 -0.1172 0.1173  -0.0482 138 LYS B CE  
3966 N NZ  . LYS B 137 ? 1.2588 0.5130 0.4081 -0.1237 0.1290  -0.0502 138 LYS B NZ  
3967 N N   . ASP B 138 ? 0.8815 0.3611 0.2488 -0.0957 0.0063  -0.0552 139 ASP B N   
3968 C CA  . ASP B 138 ? 0.8997 0.3914 0.2828 -0.0944 -0.0142 -0.0591 139 ASP B CA  
3969 C C   . ASP B 138 ? 0.8350 0.3696 0.2700 -0.0901 -0.0159 -0.0622 139 ASP B C   
3970 O O   . ASP B 138 ? 0.8570 0.4034 0.3109 -0.0892 -0.0287 -0.0666 139 ASP B O   
3971 C CB  . ASP B 138 ? 0.8963 0.3795 0.2677 -0.0934 -0.0490 -0.0527 139 ASP B CB  
3972 C CG  . ASP B 138 ? 0.9981 0.4352 0.3158 -0.0978 -0.0507 -0.0499 139 ASP B CG  
3973 O OD1 . ASP B 138 ? 1.0283 0.4380 0.3160 -0.1023 -0.0269 -0.0545 139 ASP B OD1 
3974 O OD2 . ASP B 138 ? 1.0373 0.4645 0.3439 -0.0969 -0.0756 -0.0432 139 ASP B OD2 
3975 N N   . TRP B 139 ? 0.8045 0.3606 0.2622 -0.0877 -0.0028 -0.0604 140 TRP B N   
3976 C CA  . TRP B 139 ? 0.7800 0.3746 0.2855 -0.0838 -0.0038 -0.0629 140 TRP B CA  
3977 C C   . TRP B 139 ? 0.7482 0.3544 0.2807 -0.0833 0.0128  -0.0704 140 TRP B C   
3978 O O   . TRP B 139 ? 0.7500 0.3319 0.2599 -0.0872 0.0381  -0.0776 140 TRP B O   
3979 C CB  . TRP B 139 ? 0.6959 0.3149 0.2291 -0.0802 0.0124  -0.0568 140 TRP B CB  
3980 C CG  . TRP B 139 ? 0.6716 0.3437 0.2735 -0.0729 0.0111  -0.0524 140 TRP B CG  
3981 C CD1 . TRP B 139 ? 0.6150 0.3171 0.2477 -0.0680 -0.0087 -0.0444 140 TRP B CD1 
3982 C CD2 . TRP B 139 ? 0.6189 0.3184 0.2655 -0.0698 0.0310  -0.0553 140 TRP B CD2 
3983 N NE1 . TRP B 139 ? 0.5604 0.3046 0.2497 -0.0623 -0.0021 -0.0425 140 TRP B NE1 
3984 C CE2 . TRP B 139 ? 0.5879 0.3316 0.2869 -0.0631 0.0208  -0.0487 140 TRP B CE2 
3985 C CE3 . TRP B 139 ? 0.6512 0.3408 0.2987 -0.0719 0.0563  -0.0629 140 TRP B CE3 
3986 C CZ2 . TRP B 139 ? 0.5371 0.3137 0.2858 -0.0586 0.0330  -0.0489 140 TRP B CZ2 
3987 C CZ3 . TRP B 139 ? 0.6055 0.3299 0.3073 -0.0672 0.0681  -0.0630 140 TRP B CZ3 
3988 C CH2 . TRP B 139 ? 0.5387 0.3057 0.2890 -0.0606 0.0556  -0.0558 140 TRP B CH2 
3989 N N   . LYS B 140 ? 0.6874 0.3300 0.2695 -0.0785 -0.0007 -0.0686 141 LYS B N   
3990 C CA  . LYS B 140 ? 0.6572 0.3173 0.2742 -0.0767 0.0125  -0.0739 141 LYS B CA  
3991 C C   . LYS B 140 ? 0.5928 0.3044 0.2753 -0.0691 0.0108  -0.0671 141 LYS B C   
3992 O O   . LYS B 140 ? 0.6075 0.3392 0.3067 -0.0657 -0.0076 -0.0595 141 LYS B O   
3993 C CB  . LYS B 140 ? 0.7005 0.3453 0.3048 -0.0795 -0.0044 -0.0798 141 LYS B CB  
3994 C CG  . LYS B 140 ? 0.7677 0.3584 0.3046 -0.0874 -0.0015 -0.0881 141 LYS B CG  
3995 C CD  . LYS B 140 ? 0.8769 0.4517 0.4037 -0.0900 0.0339  -0.0952 141 LYS B CD  
3996 C CE  . LYS B 140 ? 0.8642 0.4600 0.4338 -0.0878 0.0447  -0.1008 141 LYS B CE  
3997 N NZ  . LYS B 140 ? 0.7741 0.3874 0.3772 -0.0852 0.0771  -0.1016 141 LYS B NZ  
3998 N N   . PRO B 141 ? 0.5932 0.3252 0.3128 -0.0664 0.0296  -0.0695 142 PRO B N   
3999 C CA  . PRO B 141 ? 0.5478 0.3253 0.3251 -0.0592 0.0275  -0.0627 142 PRO B CA  
4000 C C   . PRO B 141 ? 0.5079 0.3049 0.3109 -0.0562 0.0056  -0.0600 142 PRO B C   
4001 O O   . PRO B 141 ? 0.5327 0.3126 0.3208 -0.0593 -0.0031 -0.0651 142 PRO B O   
4002 C CB  . PRO B 141 ? 0.5272 0.3138 0.3314 -0.0579 0.0531  -0.0668 142 PRO B CB  
4003 C CG  . PRO B 141 ? 0.5899 0.3416 0.3608 -0.0637 0.0624  -0.0765 142 PRO B CG  
4004 C CD  . PRO B 141 ? 0.5891 0.3021 0.2997 -0.0696 0.0540  -0.0783 142 PRO B CD  
4005 N N   . LYS B 142 ? 0.4417 0.2737 0.2838 -0.0503 -0.0026 -0.0521 143 LYS B N   
4006 C CA  . LYS B 142 ? 0.4202 0.2751 0.2955 -0.0465 -0.0183 -0.0486 143 LYS B CA  
4007 C C   . LYS B 142 ? 0.3630 0.2503 0.2849 -0.0407 -0.0070 -0.0453 143 LYS B C   
4008 O O   . LYS B 142 ? 0.3800 0.2700 0.3181 -0.0402 -0.0002 -0.0486 143 LYS B O   
4009 C CB  . LYS B 142 ? 0.4196 0.2839 0.2979 -0.0447 -0.0397 -0.0419 143 LYS B CB  
4010 C CG  . LYS B 142 ? 0.4332 0.3163 0.3438 -0.0417 -0.0554 -0.0390 143 LYS B CG  
4011 C CD  . LYS B 142 ? 0.4238 0.3106 0.3359 -0.0409 -0.0765 -0.0336 143 LYS B CD  
4012 C CE  . LYS B 142 ? 0.4122 0.3214 0.3416 -0.0364 -0.0734 -0.0264 143 LYS B CE  
4013 N NZ  . LYS B 142 ? 0.4168 0.3277 0.3494 -0.0358 -0.0935 -0.0218 143 LYS B NZ  
4014 N N   . ASN B 143 ? 0.3469 0.2575 0.2897 -0.0363 -0.0058 -0.0386 144 ASN B N   
4015 C CA  . ASN B 143 ? 0.3292 0.2671 0.3114 -0.0309 0.0039  -0.0352 144 ASN B CA  
4016 C C   . ASN B 143 ? 0.3662 0.2971 0.3484 -0.0322 0.0253  -0.0398 144 ASN B C   
4017 O O   . ASN B 143 ? 0.4014 0.3090 0.3535 -0.0367 0.0344  -0.0443 144 ASN B O   
4018 C CB  . ASN B 143 ? 0.3087 0.2709 0.3101 -0.0262 -0.0025 -0.0273 144 ASN B CB  
4019 C CG  . ASN B 143 ? 0.3050 0.2795 0.3191 -0.0237 -0.0201 -0.0221 144 ASN B CG  
4020 O OD1 . ASN B 143 ? 0.3133 0.2963 0.3472 -0.0218 -0.0233 -0.0214 144 ASN B OD1 
4021 N ND2 . ASN B 143 ? 0.3010 0.2767 0.3062 -0.0236 -0.0305 -0.0186 144 ASN B ND2 
4022 N N   . SER B 144 ? 0.3034 0.2535 0.3207 -0.0281 0.0337  -0.0382 145 SER B N   
4023 C CA  . SER B 144 ? 0.3280 0.2767 0.3560 -0.0282 0.0533  -0.0414 145 SER B CA  
4024 C C   . SER B 144 ? 0.3508 0.3013 0.3725 -0.0284 0.0574  -0.0394 145 SER B C   
4025 O O   . SER B 144 ? 0.3179 0.2869 0.3504 -0.0249 0.0465  -0.0330 145 SER B O   
4026 C CB  . SER B 144 ? 0.3080 0.2806 0.3789 -0.0227 0.0567  -0.0380 145 SER B CB  
4027 O OG  . SER B 144 ? 0.3913 0.3601 0.4679 -0.0229 0.0550  -0.0402 145 SER B OG  
4028 N N   . ILE B 145 ? 0.3677 0.2978 0.3723 -0.0326 0.0744  -0.0451 146 ILE B N   
4029 C CA  . ILE B 145 ? 0.3425 0.2702 0.3378 -0.0337 0.0793  -0.0438 146 ILE B CA  
4030 C C   . ILE B 145 ? 0.3158 0.2728 0.3527 -0.0283 0.0802  -0.0389 146 ILE B C   
4031 O O   . ILE B 145 ? 0.2994 0.2681 0.3689 -0.0256 0.0883  -0.0397 146 ILE B O   
4032 C CB  . ILE B 145 ? 0.3868 0.2840 0.3559 -0.0396 0.1006  -0.0511 146 ILE B CB  
4033 C CG1 . ILE B 145 ? 0.3873 0.2515 0.3055 -0.0453 0.0955  -0.0551 146 ILE B CG1 
4034 C CG2 . ILE B 145 ? 0.3816 0.2786 0.3503 -0.0403 0.1095  -0.0496 146 ILE B CG2 
4035 C CD1 . ILE B 145 ? 0.4390 0.2681 0.3270 -0.0514 0.1179  -0.0636 146 ILE B CD1 
4036 N N   . GLY B 146 ? 0.2889 0.2572 0.3252 -0.0266 0.0702  -0.0338 147 GLY B N   
4037 C CA  . GLY B 146 ? 0.3044 0.2976 0.3742 -0.0220 0.0686  -0.0296 147 GLY B CA  
4038 C C   . GLY B 146 ? 0.2951 0.3129 0.3866 -0.0162 0.0522  -0.0231 147 GLY B C   
4039 O O   . GLY B 146 ? 0.2807 0.3165 0.3915 -0.0126 0.0471  -0.0191 147 GLY B O   
4040 N N   . GLU B 147 ? 0.2733 0.2909 0.3606 -0.0154 0.0439  -0.0220 148 GLU B N   
4041 C CA  A GLU B 147 ? 0.2589 0.2975 0.3683 -0.0100 0.0322  -0.0159 148 GLU B CA  
4042 C CA  B GLU B 147 ? 0.2563 0.2952 0.3660 -0.0100 0.0322  -0.0159 148 GLU B CA  
4043 C C   . GLU B 147 ? 0.2730 0.3179 0.3715 -0.0086 0.0171  -0.0110 148 GLU B C   
4044 O O   . GLU B 147 ? 0.2312 0.2934 0.3466 -0.0040 0.0094  -0.0054 148 GLU B O   
4045 C CB  A GLU B 147 ? 0.2588 0.2949 0.3760 -0.0095 0.0331  -0.0171 148 GLU B CB  
4046 C CB  B GLU B 147 ? 0.2576 0.2949 0.3774 -0.0093 0.0340  -0.0171 148 GLU B CB  
4047 C CG  A GLU B 147 ? 0.2557 0.3121 0.3997 -0.0036 0.0253  -0.0106 148 GLU B CG  
4048 C CG  B GLU B 147 ? 0.2690 0.2995 0.4025 -0.0106 0.0503  -0.0224 148 GLU B CG  
4049 C CD  A GLU B 147 ? 0.2950 0.3483 0.4454 -0.0033 0.0250  -0.0111 148 GLU B CD  
4050 C CD  B GLU B 147 ? 0.3163 0.3514 0.4707 -0.0082 0.0517  -0.0220 148 GLU B CD  
4051 O OE1 A GLU B 147 ? 0.2883 0.3241 0.4212 -0.0078 0.0284  -0.0169 148 GLU B OE1 
4052 O OE1 B GLU B 147 ? 0.2823 0.3221 0.4356 -0.0065 0.0411  -0.0185 148 GLU B OE1 
4053 O OE2 A GLU B 147 ? 0.2772 0.3442 0.4491 0.0014  0.0210  -0.0057 148 GLU B OE2 
4054 O OE2 B GLU B 147 ? 0.3205 0.3544 0.4947 -0.0079 0.0641  -0.0252 148 GLU B OE2 
4055 N N   . TYR B 148 ? 0.2290 0.2588 0.2996 -0.0125 0.0129  -0.0127 149 TYR B N   
4056 C CA  . TYR B 148 ? 0.2271 0.2620 0.2910 -0.0113 -0.0013 -0.0083 149 TYR B CA  
4057 C C   . TYR B 148 ? 0.2655 0.2938 0.3115 -0.0134 -0.0029 -0.0081 149 TYR B C   
4058 O O   . TYR B 148 ? 0.2662 0.2745 0.2883 -0.0180 0.0024  -0.0120 149 TYR B O   
4059 C CB  . TYR B 148 ? 0.2450 0.2686 0.2968 -0.0135 -0.0097 -0.0094 149 TYR B CB  
4060 C CG  . TYR B 148 ? 0.2495 0.2864 0.3253 -0.0099 -0.0121 -0.0068 149 TYR B CG  
4061 C CD1 . TYR B 148 ? 0.2486 0.2847 0.3358 -0.0096 -0.0027 -0.0094 149 TYR B CD1 
4062 C CD2 . TYR B 148 ? 0.2342 0.2839 0.3226 -0.0065 -0.0220 -0.0013 149 TYR B CD2 
4063 C CE1 . TYR B 148 ? 0.2265 0.2741 0.3360 -0.0060 -0.0044 -0.0062 149 TYR B CE1 
4064 C CE2 . TYR B 148 ? 0.2451 0.3054 0.3546 -0.0031 -0.0222 0.0018  149 TYR B CE2 
4065 C CZ  . TYR B 148 ? 0.2178 0.2769 0.3369 -0.0029 -0.0141 -0.0004 149 TYR B CZ  
4066 O OH  . TYR B 148 ? 0.2673 0.3356 0.4067 0.0005  -0.0143 0.0033  149 TYR B OH  
4067 N N   . ARG B 149 ? 0.1771 0.2202 0.2327 -0.0102 -0.0100 -0.0034 150 ARG B N   
4068 C CA  . ARG B 149 ? 0.2104 0.2490 0.2520 -0.0116 -0.0129 -0.0025 150 ARG B CA  
4069 C C   . ARG B 149 ? 0.2381 0.2696 0.2663 -0.0127 -0.0259 -0.0005 150 ARG B C   
4070 O O   . ARG B 149 ? 0.2283 0.2711 0.2706 -0.0097 -0.0340 0.0029  150 ARG B O   
4071 C CB  . ARG B 149 ? 0.2047 0.2618 0.2642 -0.0078 -0.0138 0.0007  150 ARG B CB  
4072 C CG  . ARG B 149 ? 0.1954 0.2487 0.2428 -0.0091 -0.0169 0.0016  150 ARG B CG  
4073 C CD  . ARG B 149 ? 0.1691 0.2404 0.2331 -0.0050 -0.0205 0.0047  150 ARG B CD  
4074 N NE  . ARG B 149 ? 0.1719 0.2402 0.2277 -0.0063 -0.0213 0.0048  150 ARG B NE  
4075 C CZ  . ARG B 149 ? 0.2365 0.3026 0.2844 -0.0063 -0.0295 0.0073  150 ARG B CZ  
4076 N NH1 . ARG B 149 ? 0.2231 0.2884 0.2702 -0.0055 -0.0376 0.0096  150 ARG B NH1 
4077 N NH2 . ARG B 149 ? 0.2130 0.2777 0.2566 -0.0071 -0.0293 0.0075  150 ARG B NH2 
4078 N N   . GLN B 150 ? 0.2759 0.2875 0.2776 -0.0169 -0.0277 -0.0022 151 GLN B N   
4079 C CA  . GLN B 150 ? 0.2690 0.2732 0.2595 -0.0178 -0.0422 0.0003  151 GLN B CA  
4080 C C   . GLN B 150 ? 0.2898 0.2831 0.2613 -0.0200 -0.0420 0.0010  151 GLN B C   
4081 O O   . GLN B 150 ? 0.3284 0.3012 0.2749 -0.0241 -0.0349 -0.0020 151 GLN B O   
4082 C CB  . GLN B 150 ? 0.3017 0.2872 0.2751 -0.0212 -0.0495 -0.0024 151 GLN B CB  
4083 C CG  . GLN B 150 ? 0.3387 0.3171 0.3054 -0.0219 -0.0673 0.0005  151 GLN B CG  
4084 C CD  . GLN B 150 ? 0.4230 0.3979 0.3961 -0.0225 -0.0787 -0.0004 151 GLN B CD  
4085 O OE1 . GLN B 150 ? 0.4463 0.4183 0.4202 -0.0234 -0.0732 -0.0041 151 GLN B OE1 
4086 N NE2 . GLN B 150 ? 0.4977 0.4730 0.4781 -0.0219 -0.0946 0.0027  151 GLN B NE2 
4087 N N   . TYR B 151 ? 0.2748 0.2806 0.2582 -0.0173 -0.0480 0.0050  152 TYR B N   
4088 C CA  . TYR B 151 ? 0.3046 0.3019 0.2737 -0.0189 -0.0475 0.0062  152 TYR B CA  
4089 C C   . TYR B 151 ? 0.3072 0.2768 0.2435 -0.0235 -0.0545 0.0058  152 TYR B C   
4090 O O   . TYR B 151 ? 0.3342 0.2976 0.2670 -0.0238 -0.0687 0.0072  152 TYR B O   
4091 C CB  . TYR B 151 ? 0.2923 0.3059 0.2799 -0.0152 -0.0551 0.0103  152 TYR B CB  
4092 C CG  . TYR B 151 ? 0.3188 0.3282 0.2985 -0.0161 -0.0534 0.0116  152 TYR B CG  
4093 C CD1 . TYR B 151 ? 0.3038 0.3175 0.2864 -0.0164 -0.0408 0.0095  152 TYR B CD1 
4094 C CD2 . TYR B 151 ? 0.3809 0.3827 0.3538 -0.0165 -0.0648 0.0149  152 TYR B CD2 
4095 C CE1 . TYR B 151 ? 0.3524 0.3624 0.3298 -0.0173 -0.0388 0.0105  152 TYR B CE1 
4096 C CE2 . TYR B 151 ? 0.4043 0.4019 0.3708 -0.0172 -0.0630 0.0164  152 TYR B CE2 
4097 C CZ  . TYR B 151 ? 0.3939 0.3957 0.3623 -0.0176 -0.0494 0.0141  152 TYR B CZ  
4098 O OH  . TYR B 151 ? 0.4389 0.4369 0.4033 -0.0185 -0.0468 0.0152  152 TYR B OH  
4099 N N   . SER B 152 ? 0.3411 0.2921 0.2529 -0.0271 -0.0447 0.0040  153 SER B N   
4100 C CA  . SER B 152 ? 0.3807 0.2996 0.2536 -0.0321 -0.0489 0.0030  153 SER B CA  
4101 C C   . SER B 152 ? 0.3873 0.2870 0.2346 -0.0352 -0.0416 0.0039  153 SER B C   
4102 O O   . SER B 152 ? 0.3853 0.2855 0.2345 -0.0362 -0.0236 0.0015  153 SER B O   
4103 C CB  . SER B 152 ? 0.3950 0.3005 0.2543 -0.0350 -0.0397 -0.0025 153 SER B CB  
4104 O OG  . SER B 152 ? 0.4260 0.2962 0.2416 -0.0402 -0.0424 -0.0041 153 SER B OG  
4105 N N   . ASN B 153 ? 0.4194 0.3000 0.2427 -0.0370 -0.0554 0.0075  154 ASN B N   
4106 C CA  . ASN B 153 ? 0.4393 0.2967 0.2329 -0.0403 -0.0493 0.0093  154 ASN B CA  
4107 C C   . ASN B 153 ? 0.4792 0.3030 0.2316 -0.0458 -0.0368 0.0053  154 ASN B C   
4108 O O   . ASN B 153 ? 0.5069 0.3197 0.2475 -0.0482 -0.0185 0.0042  154 ASN B O   
4109 C CB  . ASN B 153 ? 0.4759 0.3224 0.2574 -0.0401 -0.0695 0.0153  154 ASN B CB  
4110 C CG  . ASN B 153 ? 0.4544 0.3298 0.2734 -0.0353 -0.0751 0.0190  154 ASN B CG  
4111 O OD1 . ASN B 153 ? 0.4385 0.3319 0.2780 -0.0335 -0.0615 0.0180  154 ASN B OD1 
4112 N ND2 . ASN B 153 ? 0.4691 0.3488 0.2990 -0.0332 -0.0951 0.0228  154 ASN B ND2 
4113 N N   . PRO B 154 ? 0.5454 0.3505 0.2748 -0.0483 -0.0448 0.0027  155 PRO B N   
4114 C CA  . PRO B 154 ? 0.5357 0.3071 0.2243 -0.0538 -0.0296 -0.0022 155 PRO B CA  
4115 C C   . PRO B 154 ? 0.5295 0.3126 0.2377 -0.0538 -0.0033 -0.0075 155 PRO B C   
4116 O O   . PRO B 154 ? 0.5429 0.3009 0.2242 -0.0580 0.0163  -0.0105 155 PRO B O   
4117 C CB  . PRO B 154 ? 0.5931 0.3486 0.2623 -0.0558 -0.0454 -0.0048 155 PRO B CB  
4118 C CG  . PRO B 154 ? 0.5746 0.3606 0.2832 -0.0509 -0.0655 -0.0019 155 PRO B CG  
4119 C CD  . PRO B 154 ? 0.5025 0.3104 0.2370 -0.0470 -0.0686 0.0040  155 PRO B CD  
4120 N N   . SER B 155 ? 0.4729 0.2917 0.2273 -0.0492 -0.0022 -0.0087 156 SER B N   
4121 C CA  . SER B 155 ? 0.4949 0.3265 0.2733 -0.0487 0.0200  -0.0133 156 SER B CA  
4122 C C   . SER B 155 ? 0.4531 0.2865 0.2389 -0.0491 0.0364  -0.0124 156 SER B C   
4123 O O   . SER B 155 ? 0.4655 0.2818 0.2400 -0.0526 0.0580  -0.0164 156 SER B O   
4124 C CB  . SER B 155 ? 0.4358 0.3047 0.2609 -0.0432 0.0140  -0.0131 156 SER B CB  
4125 O OG  . SER B 155 ? 0.4376 0.3167 0.2856 -0.0426 0.0325  -0.0175 156 SER B OG  
4126 N N   . ILE B 156 ? 0.4325 0.2864 0.2396 -0.0458 0.0275  -0.0077 157 ILE B N   
4127 C CA  . ILE B 156 ? 0.4368 0.2922 0.2526 -0.0465 0.0425  -0.0073 157 ILE B CA  
4128 C C   . ILE B 156 ? 0.4793 0.2980 0.2497 -0.0515 0.0478  -0.0054 157 ILE B C   
4129 O O   . ILE B 156 ? 0.5121 0.3209 0.2805 -0.0539 0.0669  -0.0066 157 ILE B O   
4130 C CB  . ILE B 156 ? 0.4497 0.3377 0.3026 -0.0415 0.0328  -0.0038 157 ILE B CB  
4131 C CG1 . ILE B 156 ? 0.4422 0.3379 0.3161 -0.0418 0.0498  -0.0053 157 ILE B CG1 
4132 C CG2 . ILE B 156 ? 0.4795 0.3626 0.3173 -0.0408 0.0140  0.0019  157 ILE B CG2 
4133 C CD1 . ILE B 156 ? 0.4112 0.3383 0.3217 -0.0371 0.0409  -0.0032 157 ILE B CD1 
4134 N N   . GLY B 157 ? 0.4956 0.2915 0.2291 -0.0533 0.0314  -0.0025 158 GLY B N   
4135 C CA  . GLY B 157 ? 0.5677 0.3229 0.2509 -0.0584 0.0361  -0.0006 158 GLY B CA  
4136 C C   . GLY B 157 ? 0.5818 0.3074 0.2368 -0.0636 0.0607  -0.0064 158 GLY B C   
4137 O O   . GLY B 157 ? 0.5956 0.2964 0.2268 -0.0674 0.0783  -0.0060 158 GLY B O   
4138 N N   . LEU B 158 ? 0.5893 0.3160 0.2471 -0.0640 0.0636  -0.0120 159 LEU B N   
4139 C CA  . LEU B 158 ? 0.5717 0.2717 0.2075 -0.0687 0.0895  -0.0184 159 LEU B CA  
4140 C C   . LEU B 158 ? 0.5948 0.3122 0.2695 -0.0680 0.1152  -0.0212 159 LEU B C   
4141 O O   . LEU B 158 ? 0.6545 0.3453 0.3097 -0.0724 0.1406  -0.0243 159 LEU B O   
4142 C CB  . LEU B 158 ? 0.5728 0.2725 0.2078 -0.0689 0.0858  -0.0239 159 LEU B CB  
4143 C CG  . LEU B 158 ? 0.6140 0.2850 0.2261 -0.0738 0.1119  -0.0317 159 LEU B CG  
4144 C CD1 . LEU B 158 ? 0.7029 0.3217 0.2486 -0.0803 0.1208  -0.0317 159 LEU B CD1 
4145 C CD2 . LEU B 158 ? 0.6308 0.3050 0.2460 -0.0733 0.1043  -0.0368 159 LEU B CD2 
4146 N N   . PHE B 159 ? 0.5180 0.2784 0.2477 -0.0625 0.1090  -0.0202 160 PHE B N   
4147 C CA  . PHE B 159 ? 0.5045 0.2836 0.2757 -0.0614 0.1287  -0.0224 160 PHE B CA  
4148 C C   . PHE B 159 ? 0.5588 0.3224 0.3168 -0.0640 0.1395  -0.0194 160 PHE B C   
4149 O O   . PHE B 159 ? 0.5328 0.2844 0.2963 -0.0670 0.1653  -0.0228 160 PHE B O   
4150 C CB  . PHE B 159 ? 0.4718 0.2968 0.2973 -0.0549 0.1147  -0.0210 160 PHE B CB  
4151 C CG  . PHE B 159 ? 0.4828 0.3289 0.3537 -0.0534 0.1295  -0.0229 160 PHE B CG  
4152 C CD1 . PHE B 159 ? 0.4848 0.3344 0.3818 -0.0540 0.1488  -0.0286 160 PHE B CD1 
4153 C CD2 . PHE B 159 ? 0.4614 0.3241 0.3514 -0.0513 0.1228  -0.0193 160 PHE B CD2 
4154 C CE1 . PHE B 159 ? 0.4339 0.3031 0.3765 -0.0526 0.1601  -0.0305 160 PHE B CE1 
4155 C CE2 . PHE B 159 ? 0.4125 0.2944 0.3456 -0.0501 0.1339  -0.0215 160 PHE B CE2 
4156 C CZ  . PHE B 159 ? 0.4336 0.3189 0.3938 -0.0507 0.1518  -0.0270 160 PHE B CZ  
4157 N N   . GLY B 160 ? 0.5572 0.3202 0.3000 -0.0629 0.1207  -0.0130 161 GLY B N   
4158 C CA  . GLY B 160 ? 0.5698 0.3169 0.2988 -0.0653 0.1298  -0.0095 161 GLY B CA  
4159 C C   . GLY B 160 ? 0.6573 0.3553 0.3315 -0.0719 0.1486  -0.0102 161 GLY B C   
4160 O O   . GLY B 160 ? 0.6665 0.3501 0.3393 -0.0749 0.1712  -0.0106 161 GLY B O   
4161 N N   . LYS B 161 ? 0.6786 0.3485 0.3059 -0.0744 0.1398  -0.0105 162 LYS B N   
4162 C CA  . LYS B 161 ? 0.7411 0.3595 0.3091 -0.0810 0.1577  -0.0117 162 LYS B CA  
4163 C C   . LYS B 161 ? 0.7454 0.3590 0.3337 -0.0829 0.1889  -0.0195 162 LYS B C   
4164 O O   . LYS B 161 ? 0.7834 0.3706 0.3584 -0.0854 0.2059  -0.0209 162 LYS B O   
4165 C CB  . LYS B 161 ? 0.7795 0.3736 0.3034 -0.0823 0.1378  -0.0120 162 LYS B CB  
4166 C CG  . LYS B 161 ? 0.8842 0.4333 0.3668 -0.0866 0.1489  -0.0148 162 LYS B CG  
4167 C CD  . LYS B 161 ? 0.9429 0.4672 0.3828 -0.0879 0.1237  -0.0131 162 LYS B CD  
4168 C CE  . LYS B 161 ? 0.9990 0.4751 0.3933 -0.0927 0.1341  -0.0147 162 LYS B CE  
4169 N NZ  . LYS B 161 ? 0.9801 0.4387 0.3620 -0.0936 0.1433  -0.0108 162 LYS B NZ  
4170 N N   . VAL B 162 ? 0.7121 0.3509 0.3357 -0.0812 0.1955  -0.0249 163 VAL B N   
4171 C CA  . VAL B 162 ? 0.6890 0.3272 0.3417 -0.0822 0.2223  -0.0323 163 VAL B CA  
4172 C C   . VAL B 162 ? 0.7001 0.3566 0.3987 -0.0809 0.2384  -0.0323 163 VAL B C   
4173 O O   . VAL B 162 ? 0.7113 0.3505 0.4177 -0.0827 0.2597  -0.0365 163 VAL B O   
4174 C CB  . VAL B 162 ? 0.7164 0.3792 0.3986 -0.0800 0.2219  -0.0375 163 VAL B CB  
4175 C CG1 . VAL B 162 ? 0.6983 0.3705 0.4275 -0.0797 0.2465  -0.0439 163 VAL B CG1 
4176 C CG2 . VAL B 162 ? 0.7403 0.3781 0.3772 -0.0821 0.2105  -0.0397 163 VAL B CG2 
4177 N N   . VAL B 163 ? 0.6060 0.2974 0.3385 -0.0777 0.2270  -0.0280 164 VAL B N   
4178 C CA  . VAL B 163 ? 0.6865 0.3945 0.4617 -0.0769 0.2399  -0.0278 164 VAL B CA  
4179 C C   . VAL B 163 ? 0.6988 0.3727 0.4417 -0.0795 0.2490  -0.0260 164 VAL B C   
4180 O O   . VAL B 163 ? 0.7210 0.3883 0.4864 -0.0798 0.2687  -0.0302 164 VAL B O   
4181 C CB  . VAL B 163 ? 0.5804 0.3307 0.3957 -0.0711 0.2146  -0.0236 164 VAL B CB  
4182 C CG1 . VAL B 163 ? 0.6133 0.3731 0.4605 -0.0714 0.2261  -0.0228 164 VAL B CG1 
4183 C CG2 . VAL B 163 ? 0.5578 0.3460 0.4197 -0.0660 0.2030  -0.0269 164 VAL B CG2 
4184 N N   . ALA B 164 ? 0.7024 0.3530 0.3929 -0.0810 0.2338  -0.0199 165 ALA B N   
4185 C CA  . ALA B 164 ? 0.7484 0.3650 0.4051 -0.0832 0.2407  -0.0177 165 ALA B CA  
4186 C C   . ALA B 164 ? 0.8284 0.4073 0.4602 -0.0864 0.2607  -0.0239 165 ALA B C   
4187 O O   . ALA B 164 ? 0.8644 0.4222 0.4921 -0.0878 0.2781  -0.0253 165 ALA B O   
4188 C CB  . ALA B 164 ? 0.7760 0.3762 0.3841 -0.0836 0.2159  -0.0096 165 ALA B CB  
4189 N N   . LEU B 165 ? 0.7880 0.3566 0.4030 -0.0878 0.2595  -0.0278 166 LEU B N   
4190 C CA  . LEU B 165 ? 0.8506 0.3829 0.4449 -0.0915 0.2803  -0.0337 166 LEU B CA  
4191 C C   . LEU B 165 ? 0.8388 0.3831 0.4857 -0.0907 0.3063  -0.0400 166 LEU B C   
4192 O O   . LEU B 165 ? 0.9072 0.4214 0.5441 -0.0932 0.3272  -0.0431 166 LEU B O   
4193 C CB  . LEU B 165 ? 0.8672 0.3890 0.4384 -0.0933 0.2736  -0.0367 166 LEU B CB  
4194 C CG  . LEU B 165 ? 0.8946 0.3924 0.4073 -0.0949 0.2491  -0.0321 166 LEU B CG  
4195 C CD1 . LEU B 165 ? 0.9121 0.4027 0.4110 -0.0966 0.2449  -0.0362 166 LEU B CD1 
4196 C CD2 . LEU B 165 ? 0.9680 0.4198 0.4303 -0.0984 0.2531  -0.0297 166 LEU B CD2 
4197 N N   . SER B 166 ? 0.8076 0.3948 0.5121 -0.0870 0.3044  -0.0419 167 SER B N   
4198 C CA  . SER B 166 ? 0.8028 0.4035 0.5630 -0.0856 0.3248  -0.0479 167 SER B CA  
4199 C C   . SER B 166 ? 0.8313 0.4296 0.6084 -0.0849 0.3354  -0.0471 167 SER B C   
4200 O O   . SER B 166 ? 0.8103 0.4066 0.6233 -0.0844 0.3550  -0.0525 167 SER B O   
4201 C CB  . SER B 166 ? 0.7637 0.4126 0.5831 -0.0812 0.3155  -0.0492 167 SER B CB  
4202 O OG  . SER B 166 ? 0.7173 0.3979 0.5621 -0.0781 0.3015  -0.0443 167 SER B OG  
4203 N N   . MET B 167 ? 0.7894 0.3881 0.5436 -0.0845 0.3223  -0.0404 168 MET B N   
4204 C CA  . MET B 167 ? 0.8640 0.4604 0.6314 -0.0839 0.3310  -0.0389 168 MET B CA  
4205 C C   . MET B 167 ? 0.9495 0.4984 0.6586 -0.0873 0.3396  -0.0370 168 MET B C   
4206 O O   . MET B 167 ? 0.9437 0.4863 0.6585 -0.0869 0.3481  -0.0357 168 MET B O   
4207 C CB  . MET B 167 ? 0.8123 0.4437 0.6005 -0.0812 0.3111  -0.0325 168 MET B CB  
4208 C CG  . MET B 167 ? 0.7383 0.4162 0.5947 -0.0775 0.3065  -0.0351 168 MET B CG  
4209 S SD  . MET B 167 ? 0.8144 0.5297 0.6818 -0.0757 0.2789  -0.0273 168 MET B SD  
4210 C CE  . MET B 167 ? 0.7401 0.4997 0.6909 -0.0717 0.2799  -0.0317 168 MET B CE  
4211 N N   . ASN B 168 ? 0.9443 0.4592 0.5980 -0.0907 0.3366  -0.0367 169 ASN B N   
4212 C CA  . ASN B 168 ? 1.0178 0.4835 0.6123 -0.0942 0.3435  -0.0351 169 ASN B CA  
4213 C C   . ASN B 168 ? 1.0317 0.4966 0.6051 -0.0932 0.3289  -0.0272 169 ASN B C   
4214 O O   . ASN B 168 ? 1.0285 0.4675 0.5840 -0.0943 0.3414  -0.0264 169 ASN B O   
4215 C CB  . ASN B 168 ? 1.1069 0.5456 0.7111 -0.0961 0.3752  -0.0418 169 ASN B CB  
4216 C CG  . ASN B 168 ? 1.1831 0.6303 0.8245 -0.0965 0.3901  -0.0495 169 ASN B CG  
4217 O OD1 . ASN B 168 ? 1.1982 0.6770 0.9020 -0.0933 0.3978  -0.0531 169 ASN B OD1 
4218 N ND2 . ASN B 168 ? 1.1727 0.5917 0.7771 -0.1003 0.3927  -0.0518 169 ASN B ND2 
4219 N N   . LYS B 169 ? 0.9482 0.4410 0.5247 -0.0910 0.3027  -0.0211 170 LYS B N   
4220 C CA  . LYS B 169 ? 0.9399 0.4336 0.4975 -0.0901 0.2852  -0.0126 170 LYS B CA  
4221 C C   . LYS B 169 ? 0.9199 0.4220 0.4532 -0.0894 0.2547  -0.0070 170 LYS B C   
4222 O O   . LYS B 169 ? 0.9227 0.4486 0.4764 -0.0883 0.2476  -0.0093 170 LYS B O   
4223 C CB  . LYS B 169 ? 0.9206 0.4516 0.5330 -0.0872 0.2876  -0.0107 170 LYS B CB  
4224 C CG  . LYS B 169 ? 1.0068 0.5352 0.6539 -0.0870 0.3156  -0.0167 170 LYS B CG  
4225 C CD  . LYS B 169 ? 0.9848 0.5591 0.6995 -0.0839 0.3151  -0.0173 170 LYS B CD  
4226 C CE  . LYS B 169 ? 0.9498 0.5293 0.7123 -0.0829 0.3399  -0.0260 170 LYS B CE  
4227 N NZ  . LYS B 169 ? 0.8824 0.5088 0.7101 -0.0798 0.3335  -0.0290 170 LYS B NZ  
4228 N N   . PRO B 170 ? 0.9541 0.4374 0.4462 -0.0897 0.2356  0.0002  171 PRO B N   
4229 C CA  . PRO B 170 ? 0.8877 0.3843 0.3671 -0.0880 0.2038  0.0061  171 PRO B CA  
4230 C C   . PRO B 170 ? 0.8886 0.4328 0.4191 -0.0848 0.1958  0.0088  171 PRO B C   
4231 O O   . PRO B 170 ? 0.8237 0.3871 0.3923 -0.0840 0.2088  0.0089  171 PRO B O   
4232 C CB  . PRO B 170 ? 0.9548 0.4248 0.3927 -0.0883 0.1877  0.0135  171 PRO B CB  
4233 C CG  . PRO B 170 ? 0.9457 0.3780 0.3588 -0.0912 0.2121  0.0104  171 PRO B CG  
4234 C CD  . PRO B 170 ? 0.9502 0.4005 0.4099 -0.0911 0.2416  0.0035  171 PRO B CD  
4235 N N   . PHE B 171 ? 0.8024 0.3650 0.3347 -0.0832 0.1739  0.0108  172 PHE B N   
4236 C CA  . PHE B 171 ? 0.8032 0.4088 0.3826 -0.0807 0.1678  0.0128  172 PHE B CA  
4237 C C   . PHE B 171 ? 0.7411 0.3576 0.3349 -0.0795 0.1609  0.0202  172 PHE B C   
4238 O O   . PHE B 171 ? 0.7277 0.3767 0.3738 -0.0775 0.1679  0.0181  172 PHE B O   
4239 C CB  . PHE B 171 ? 0.7512 0.3728 0.3281 -0.0784 0.1424  0.0139  172 PHE B CB  
4240 C CG  . PHE B 171 ? 0.7115 0.3864 0.3527 -0.0722 0.1287  0.0124  172 PHE B CG  
4241 C CD1 . PHE B 171 ? 0.6556 0.3592 0.3411 -0.0704 0.1395  0.0053  172 PHE B CD1 
4242 C CD2 . PHE B 171 ? 0.6668 0.3612 0.3233 -0.0683 0.1055  0.0180  172 PHE B CD2 
4243 C CE1 . PHE B 171 ? 0.6258 0.3750 0.3654 -0.0648 0.1264  0.0042  172 PHE B CE1 
4244 C CE2 . PHE B 171 ? 0.5896 0.3291 0.3001 -0.0629 0.0946  0.0163  172 PHE B CE2 
4245 C CZ  . PHE B 171 ? 0.5528 0.3189 0.3028 -0.0612 0.1045  0.0095  172 PHE B CZ  
4246 N N   . ASP B 172 ? 0.7140 0.3090 0.2719 -0.0792 0.1428  0.0269  173 ASP B N   
4247 C CA  . ASP B 172 ? 0.7839 0.3881 0.3558 -0.0779 0.1353  0.0343  173 ASP B CA  
4248 C C   . ASP B 172 ? 0.7669 0.3713 0.3628 -0.0793 0.1621  0.0316  173 ASP B C   
4249 O O   . ASP B 172 ? 0.7485 0.3742 0.3788 -0.0783 0.1623  0.0346  173 ASP B O   
4250 C CB  . ASP B 172 ? 0.7841 0.3627 0.3146 -0.0770 0.1122  0.0412  173 ASP B CB  
4251 C CG  . ASP B 172 ? 0.9365 0.4747 0.4259 -0.0796 0.1244  0.0391  173 ASP B CG  
4252 O OD1 . ASP B 172 ? 0.9453 0.4665 0.4172 -0.0818 0.1374  0.0322  173 ASP B OD1 
4253 O OD2 . ASP B 172 ? 0.9884 0.5101 0.4623 -0.0796 0.1215  0.0445  173 ASP B OD2 
4254 N N   . GLN B 173 ? 0.7988 0.3804 0.3808 -0.0813 0.1842  0.0251  174 GLN B N   
4255 C CA  . GLN B 173 ? 0.7909 0.3722 0.3989 -0.0822 0.2103  0.0212  174 GLN B CA  
4256 C C   . GLN B 173 ? 0.7409 0.3593 0.4104 -0.0813 0.2239  0.0150  174 GLN B C   
4257 O O   . GLN B 173 ? 0.7097 0.3447 0.4189 -0.0808 0.2343  0.0141  174 GLN B O   
4258 C CB  . GLN B 173 ? 0.8865 0.4284 0.4589 -0.0844 0.2291  0.0161  174 GLN B CB  
4259 C CG  . GLN B 173 ? 0.9280 0.4329 0.4464 -0.0854 0.2189  0.0221  174 GLN B CG  
4260 C CD  . GLN B 173 ? 1.0198 0.5263 0.5502 -0.0848 0.2228  0.0273  174 GLN B CD  
4261 O OE1 . GLN B 173 ? 1.0506 0.5609 0.5727 -0.0835 0.2018  0.0356  174 GLN B OE1 
4262 N NE2 . GLN B 173 ? 1.1019 0.6052 0.6547 -0.0855 0.2498  0.0222  174 GLN B NE2 
4263 N N   . VAL B 174 ? 0.7536 0.3850 0.4335 -0.0810 0.2231  0.0102  175 VAL B N   
4264 C CA  . VAL B 174 ? 0.6406 0.3091 0.3812 -0.0798 0.2323  0.0043  175 VAL B CA  
4265 C C   . VAL B 174 ? 0.6367 0.3406 0.4186 -0.0776 0.2183  0.0078  175 VAL B C   
4266 O O   . VAL B 174 ? 0.6183 0.3456 0.4513 -0.0769 0.2285  0.0038  175 VAL B O   
4267 C CB  . VAL B 174 ? 0.6983 0.3762 0.4392 -0.0793 0.2278  0.0003  175 VAL B CB  
4268 C CG1 . VAL B 174 ? 0.6080 0.3297 0.4143 -0.0766 0.2285  -0.0047 175 VAL B CG1 
4269 C CG2 . VAL B 174 ? 0.7451 0.3922 0.4596 -0.0808 0.2443  -0.0062 175 VAL B CG2 
4270 N N   . LEU B 175 ? 0.6210 0.3332 0.3878 -0.0741 0.1892  0.0131  176 LEU B N   
4271 C CA  . LEU B 175 ? 0.5491 0.2980 0.3579 -0.0694 0.1707  0.0139  176 LEU B CA  
4272 C C   . LEU B 175 ? 0.5962 0.3352 0.4077 -0.0711 0.1784  0.0178  176 LEU B C   
4273 O O   . LEU B 175 ? 0.5635 0.3270 0.4221 -0.0700 0.1834  0.0143  176 LEU B O   
4274 C CB  . LEU B 175 ? 0.5028 0.2632 0.2981 -0.0651 0.1395  0.0180  176 LEU B CB  
4275 C CG  . LEU B 175 ? 0.5162 0.2949 0.3199 -0.0623 0.1282  0.0140  176 LEU B CG  
4276 C CD1 . LEU B 175 ? 0.5069 0.3014 0.3085 -0.0578 0.0984  0.0180  176 LEU B CD1 
4277 C CD2 . LEU B 175 ? 0.4929 0.3053 0.3506 -0.0602 0.1361  0.0068  176 LEU B CD2 
4278 N N   . GLU B 176 ? 0.6115 0.3134 0.3725 -0.0740 0.1789  0.0252  177 GLU B N   
4279 C CA  . GLU B 176 ? 0.5993 0.2927 0.3612 -0.0748 0.1811  0.0304  177 GLU B CA  
4280 C C   . GLU B 176 ? 0.6709 0.3535 0.4512 -0.0791 0.2128  0.0273  177 GLU B C   
4281 O O   . GLU B 176 ? 0.6631 0.3567 0.4727 -0.0789 0.2157  0.0279  177 GLU B O   
4282 C CB  . GLU B 176 ? 0.6768 0.3319 0.3781 -0.0764 0.1703  0.0400  177 GLU B CB  
4283 C CG  . GLU B 176 ? 0.6682 0.3406 0.3676 -0.0713 0.1358  0.0440  177 GLU B CG  
4284 C CD  . GLU B 176 ? 0.7279 0.3624 0.3698 -0.0726 0.1213  0.0535  177 GLU B CD  
4285 O OE1 . GLU B 176 ? 0.7830 0.3795 0.3859 -0.0764 0.1363  0.0565  177 GLU B OE1 
4286 O OE2 . GLU B 176 ? 0.6923 0.3374 0.3321 -0.0688 0.0934  0.0569  177 GLU B OE2 
4287 N N   . LYS B 177 ? 0.6747 0.3438 0.4474 -0.0798 0.2311  0.0206  178 LYS B N   
4288 C CA  . LYS B 177 ? 0.7313 0.3949 0.5271 -0.0799 0.2552  0.0144  178 LYS B CA  
4289 C C   . LYS B 177 ? 0.6536 0.3473 0.5088 -0.0785 0.2666  0.0049  178 LYS B C   
4290 O O   . LYS B 177 ? 0.6714 0.3665 0.5574 -0.0778 0.2835  -0.0004 178 LYS B O   
4291 C CB  . LYS B 177 ? 0.7744 0.3954 0.5206 -0.0812 0.2698  0.0129  178 LYS B CB  
4292 C CG  . LYS B 177 ? 0.9075 0.4967 0.6049 -0.0821 0.2634  0.0211  178 LYS B CG  
4293 C CD  . LYS B 177 ? 1.0190 0.5692 0.6854 -0.0835 0.2857  0.0178  178 LYS B CD  
4294 C CE  . LYS B 177 ? 1.1120 0.6372 0.7455 -0.0841 0.2823  0.0255  178 LYS B CE  
4295 N NZ  . LYS B 177 ? 1.1789 0.6845 0.7593 -0.0844 0.2573  0.0337  178 LYS B NZ  
4296 N N   . THR B 178 ? 0.6593 0.3768 0.5329 -0.0778 0.2569  0.0026  179 THR B N   
4297 C CA  . THR B 178 ? 0.5955 0.3409 0.5254 -0.0757 0.2648  -0.0064 179 THR B CA  
4298 C C   . THR B 178 ? 0.5538 0.3406 0.5280 -0.0744 0.2469  -0.0065 179 THR B C   
4299 O O   . THR B 178 ? 0.5606 0.3723 0.5872 -0.0726 0.2475  -0.0113 179 THR B O   
4300 C CB  . THR B 178 ? 0.6462 0.3792 0.5610 -0.0756 0.2738  -0.0114 179 THR B CB  
4301 O OG1 . THR B 178 ? 0.6884 0.3807 0.5627 -0.0772 0.2914  -0.0126 179 THR B OG1 
4302 C CG2 . THR B 178 ? 0.6068 0.3676 0.5822 -0.0728 0.2802  -0.0201 179 THR B CG2 
4303 N N   . ILE B 179 ? 0.5399 0.3368 0.4949 -0.0721 0.2244  -0.0034 180 ILE B N   
4304 C CA  . ILE B 179 ? 0.5193 0.3579 0.5150 -0.0666 0.2011  -0.0065 180 ILE B CA  
4305 C C   . ILE B 179 ? 0.4929 0.3475 0.5036 -0.0642 0.1849  -0.0040 180 ILE B C   
4306 O O   . ILE B 179 ? 0.4266 0.3089 0.4848 -0.0622 0.1801  -0.0087 180 ILE B O   
4307 C CB  . ILE B 179 ? 0.5314 0.3761 0.5038 -0.0633 0.1820  -0.0053 180 ILE B CB  
4308 C CG1 . ILE B 179 ? 0.4919 0.3230 0.4546 -0.0655 0.1982  -0.0090 180 ILE B CG1 
4309 C CG2 . ILE B 179 ? 0.4515 0.3360 0.4615 -0.0576 0.1589  -0.0077 180 ILE B CG2 
4310 C CD1 . ILE B 179 ? 0.4938 0.3412 0.5091 -0.0660 0.2155  -0.0162 180 ILE B CD1 
4311 N N   . PHE B 180 ? 0.4783 0.3154 0.4494 -0.0643 0.1748  0.0031  181 PHE B N   
4312 C CA  . PHE B 180 ? 0.5080 0.3586 0.4928 -0.0620 0.1603  0.0055  181 PHE B CA  
4313 C C   . PHE B 180 ? 0.5104 0.3637 0.5302 -0.0646 0.1763  0.0023  181 PHE B C   
4314 O O   . PHE B 180 ? 0.4878 0.3682 0.5455 -0.0620 0.1649  -0.0012 181 PHE B O   
4315 C CB  . PHE B 180 ? 0.5028 0.3287 0.4397 -0.0623 0.1501  0.0142  181 PHE B CB  
4316 C CG  . PHE B 180 ? 0.4619 0.2896 0.3723 -0.0592 0.1292  0.0172  181 PHE B CG  
4317 C CD1 . PHE B 180 ? 0.4557 0.3121 0.3894 -0.0554 0.1172  0.0126  181 PHE B CD1 
4318 C CD2 . PHE B 180 ? 0.4866 0.2864 0.3496 -0.0601 0.1207  0.0250  181 PHE B CD2 
4319 C CE1 . PHE B 180 ? 0.4590 0.3168 0.3709 -0.0527 0.0988  0.0153  181 PHE B CE1 
4320 C CE2 . PHE B 180 ? 0.4811 0.2827 0.3237 -0.0574 0.1004  0.0275  181 PHE B CE2 
4321 C CZ  . PHE B 180 ? 0.4768 0.3078 0.3449 -0.0538 0.0903  0.0225  181 PHE B CZ  
4322 N N   . PRO B 181 ? 0.4991 0.3247 0.5090 -0.0697 0.2026  0.0030  182 PRO B N   
4323 C CA  . PRO B 181 ? 0.5072 0.3379 0.5583 -0.0722 0.2183  -0.0007 182 PRO B CA  
4324 C C   . PRO B 181 ? 0.5015 0.3634 0.6115 -0.0709 0.2196  -0.0099 182 PRO B C   
4325 O O   . PRO B 181 ? 0.4474 0.3285 0.6002 -0.0705 0.2164  -0.0139 182 PRO B O   
4326 C CB  . PRO B 181 ? 0.5763 0.3697 0.5979 -0.0756 0.2442  0.0010  182 PRO B CB  
4327 C CG  . PRO B 181 ? 0.5885 0.3517 0.5460 -0.0773 0.2402  0.0091  182 PRO B CG  
4328 C CD  . PRO B 181 ? 0.5551 0.3402 0.5129 -0.0738 0.2192  0.0077  182 PRO B CD  
4329 N N   . ALA B 182 ? 0.5200 0.3867 0.6341 -0.0703 0.2232  -0.0133 183 ALA B N   
4330 C CA  . ALA B 182 ? 0.4504 0.3474 0.6188 -0.0670 0.2183  -0.0217 183 ALA B CA  
4331 C C   . ALA B 182 ? 0.4070 0.3372 0.6008 -0.0633 0.1912  -0.0233 183 ALA B C   
4332 O O   . ALA B 182 ? 0.3961 0.3491 0.6389 -0.0621 0.1863  -0.0294 183 ALA B O   
4333 C CB  . ALA B 182 ? 0.4098 0.3049 0.5721 -0.0657 0.2231  -0.0242 183 ALA B CB  
4334 N N   . LEU B 183 ? 0.4053 0.3374 0.5646 -0.0600 0.1710  -0.0184 184 LEU B N   
4335 C CA  . LEU B 183 ? 0.3758 0.3353 0.5511 -0.0553 0.1453  -0.0200 184 LEU B CA  
4336 C C   . LEU B 183 ? 0.4026 0.3624 0.5820 -0.0556 0.1398  -0.0187 184 LEU B C   
4337 O O   . LEU B 183 ? 0.4143 0.3934 0.6030 -0.0520 0.1199  -0.0201 184 LEU B O   
4338 C CB  . LEU B 183 ? 0.3317 0.2939 0.4729 -0.0516 0.1276  -0.0158 184 LEU B CB  
4339 C CG  . LEU B 183 ? 0.3812 0.3462 0.5201 -0.0506 0.1298  -0.0174 184 LEU B CG  
4340 C CD1 . LEU B 183 ? 0.3132 0.2721 0.4114 -0.0483 0.1165  -0.0122 184 LEU B CD1 
4341 C CD2 . LEU B 183 ? 0.3670 0.3614 0.5500 -0.0475 0.1197  -0.0236 184 LEU B CD2 
4342 N N   . GLY B 184 ? 0.3908 0.3280 0.5617 -0.0599 0.1577  -0.0160 185 GLY B N   
4343 C CA  . GLY B 184 ? 0.4195 0.3558 0.5960 -0.0603 0.1538  -0.0147 185 GLY B CA  
4344 C C   . GLY B 184 ? 0.4843 0.4147 0.6240 -0.0577 0.1375  -0.0080 185 GLY B C   
4345 O O   . GLY B 184 ? 0.4780 0.4149 0.6271 -0.0567 0.1285  -0.0080 185 GLY B O   
4346 N N   . LEU B 185 ? 0.4287 0.3463 0.5284 -0.0567 0.1332  -0.0025 186 LEU B N   
4347 C CA  . LEU B 185 ? 0.4267 0.3386 0.4946 -0.0541 0.1165  0.0041  186 LEU B CA  
4348 C C   . LEU B 185 ? 0.4834 0.3622 0.5181 -0.0574 0.1270  0.0119  186 LEU B C   
4349 O O   . LEU B 185 ? 0.5328 0.3858 0.5423 -0.0611 0.1438  0.0146  186 LEU B O   
4350 C CB  . LEU B 185 ? 0.4324 0.3461 0.4761 -0.0515 0.1052  0.0061  186 LEU B CB  
4351 C CG  . LEU B 185 ? 0.3864 0.3282 0.4601 -0.0487 0.0986  -0.0009 186 LEU B CG  
4352 C CD1 . LEU B 185 ? 0.4017 0.3441 0.4519 -0.0463 0.0887  0.0014  186 LEU B CD1 
4353 C CD2 . LEU B 185 ? 0.3951 0.3629 0.4998 -0.0454 0.0841  -0.0052 186 LEU B CD2 
4354 N N   . LYS B 186 ? 0.4544 0.3322 0.4876 -0.0562 0.1175  0.0155  187 LYS B N   
4355 C CA  . LYS B 186 ? 0.5022 0.3489 0.5077 -0.0592 0.1266  0.0232  187 LYS B CA  
4356 C C   . LYS B 186 ? 0.4855 0.3153 0.4503 -0.0573 0.1105  0.0324  187 LYS B C   
4357 O O   . LYS B 186 ? 0.4821 0.2803 0.4143 -0.0599 0.1170  0.0402  187 LYS B O   
4358 C CB  . LYS B 186 ? 0.5278 0.3815 0.5644 -0.0600 0.1305  0.0211  187 LYS B CB  
4359 C CG  . LYS B 186 ? 0.5834 0.4433 0.6567 -0.0635 0.1504  0.0137  187 LYS B CG  
4360 C CD  . LYS B 186 ? 0.6195 0.5110 0.7413 -0.0615 0.1407  0.0052  187 LYS B CD  
4361 C CE  . LYS B 186 ? 0.6364 0.5350 0.7999 -0.0649 0.1579  -0.0026 187 LYS B CE  
4362 N NZ  . LYS B 186 ? 0.6852 0.6103 0.8775 -0.0629 0.1506  -0.0108 187 LYS B NZ  
4363 N N   . HIS B 187 ? 0.4619 0.3103 0.4280 -0.0528 0.0897  0.0320  188 HIS B N   
4364 C CA  . HIS B 187 ? 0.4786 0.3127 0.4124 -0.0507 0.0726  0.0403  188 HIS B CA  
4365 C C   . HIS B 187 ? 0.4591 0.3031 0.3829 -0.0481 0.0597  0.0393  188 HIS B C   
4366 O O   . HIS B 187 ? 0.4416 0.2976 0.3685 -0.0442 0.0407  0.0410  188 HIS B O   
4367 C CB  . HIS B 187 ? 0.4316 0.2770 0.3836 -0.0475 0.0589  0.0422  188 HIS B CB  
4368 C CG  . HIS B 187 ? 0.4755 0.3068 0.4327 -0.0502 0.0704  0.0447  188 HIS B CG  
4369 N ND1 . HIS B 187 ? 0.5005 0.3485 0.4951 -0.0512 0.0810  0.0374  188 HIS B ND1 
4370 C CD2 . HIS B 187 ? 0.5173 0.3177 0.4463 -0.0522 0.0730  0.0539  188 HIS B CD2 
4371 C CE1 . HIS B 187 ? 0.5194 0.3487 0.5111 -0.0537 0.0905  0.0417  188 HIS B CE1 
4372 N NE2 . HIS B 187 ? 0.5461 0.3459 0.4972 -0.0543 0.0863  0.0520  188 HIS B NE2 
4373 N N   . SER B 188 ? 0.4322 0.2703 0.3456 -0.0505 0.0712  0.0362  189 SER B N   
4374 C CA  . SER B 188 ? 0.4611 0.3024 0.3597 -0.0489 0.0618  0.0357  189 SER B CA  
4375 C C   . SER B 188 ? 0.4897 0.2937 0.3400 -0.0529 0.0695  0.0407  189 SER B C   
4376 O O   . SER B 188 ? 0.5237 0.3071 0.3625 -0.0573 0.0906  0.0405  189 SER B O   
4377 C CB  . SER B 188 ? 0.4395 0.3072 0.3692 -0.0480 0.0680  0.0269  189 SER B CB  
4378 O OG  . SER B 188 ? 0.4173 0.3158 0.3868 -0.0446 0.0605  0.0221  189 SER B OG  
4379 N N   . TYR B 189 ? 0.4839 0.2773 0.3056 -0.0516 0.0528  0.0452  190 TYR B N   
4380 C CA  . TYR B 189 ? 0.5436 0.2963 0.3123 -0.0554 0.0555  0.0510  190 TYR B CA  
4381 C C   . TYR B 189 ? 0.5344 0.2847 0.2833 -0.0546 0.0432  0.0502  190 TYR B C   
4382 O O   . TYR B 189 ? 0.5042 0.2803 0.2750 -0.0504 0.0256  0.0486  190 TYR B O   
4383 C CB  . TYR B 189 ? 0.5633 0.2911 0.3049 -0.0554 0.0427  0.0607  190 TYR B CB  
4384 C CG  . TYR B 189 ? 0.5604 0.2906 0.3223 -0.0557 0.0512  0.0625  190 TYR B CG  
4385 C CD1 . TYR B 189 ? 0.5967 0.3017 0.3428 -0.0604 0.0745  0.0639  190 TYR B CD1 
4386 C CD2 . TYR B 189 ? 0.5494 0.3061 0.3471 -0.0514 0.0373  0.0626  190 TYR B CD2 
4387 C CE1 . TYR B 189 ? 0.6100 0.3172 0.3770 -0.0608 0.0824  0.0654  190 TYR B CE1 
4388 C CE2 . TYR B 189 ? 0.5308 0.2895 0.3479 -0.0518 0.0448  0.0637  190 TYR B CE2 
4389 C CZ  . TYR B 189 ? 0.5826 0.3170 0.3849 -0.0564 0.0668  0.0651  190 TYR B CZ  
4390 O OH  . TYR B 189 ? 0.5562 0.2926 0.3798 -0.0569 0.0744  0.0660  190 TYR B OH  
4391 N N   . VAL B 190 ? 0.5669 0.2836 0.2723 -0.0589 0.0532  0.0512  191 VAL B N   
4392 C CA  . VAL B 190 ? 0.6203 0.3219 0.2928 -0.0590 0.0376  0.0529  191 VAL B CA  
4393 C C   . VAL B 190 ? 0.6775 0.3472 0.3094 -0.0596 0.0192  0.0625  191 VAL B C   
4394 O O   . VAL B 190 ? 0.6664 0.3401 0.2955 -0.0569 -0.0058 0.0653  191 VAL B O   
4395 C CB  . VAL B 190 ? 0.6983 0.3786 0.3430 -0.0633 0.0567  0.0482  191 VAL B CB  
4396 C CG1 . VAL B 190 ? 0.7063 0.3643 0.3098 -0.0642 0.0399  0.0501  191 VAL B CG1 
4397 C CG2 . VAL B 190 ? 0.6256 0.3410 0.3160 -0.0617 0.0695  0.0391  191 VAL B CG2 
4398 N N   . ASN B 191 ? 0.7064 0.3438 0.3084 -0.0631 0.0308  0.0679  192 ASN B N   
4399 C CA  . ASN B 191 ? 0.7437 0.3507 0.3104 -0.0634 0.0132  0.0781  192 ASN B CA  
4400 C C   . ASN B 191 ? 0.7060 0.3235 0.3002 -0.0618 0.0165  0.0819  192 ASN B C   
4401 O O   . ASN B 191 ? 0.7166 0.3259 0.3123 -0.0647 0.0408  0.0809  192 ASN B O   
4402 C CB  . ASN B 191 ? 0.7830 0.3505 0.3000 -0.0668 0.0217  0.0771  192 ASN B CB  
4403 C CG  . ASN B 191 ? 0.8480 0.4075 0.3439 -0.0684 0.0222  0.0703  192 ASN B CG  
4404 O OD1 . ASN B 191 ? 0.8453 0.4084 0.3368 -0.0664 -0.0017 0.0702  192 ASN B OD1 
4405 N ND2 . ASN B 191 ? 0.8884 0.4377 0.3755 -0.0718 0.0500  0.0638  192 ASN B ND2 
4406 N N   . VAL B 192 ? 0.6978 0.3331 0.3159 -0.0573 -0.0070 0.0859  193 VAL B N   
4407 C CA  . VAL B 192 ? 0.6798 0.3254 0.3255 -0.0555 -0.0057 0.0893  193 VAL B CA  
4408 C C   . VAL B 192 ? 0.7926 0.3926 0.3922 -0.0588 -0.0033 0.0993  193 VAL B C   
4409 O O   . VAL B 192 ? 0.8490 0.4304 0.4198 -0.0578 -0.0223 0.1028  193 VAL B O   
4410 C CB  . VAL B 192 ? 0.6557 0.3306 0.3391 -0.0497 -0.0306 0.0905  193 VAL B CB  
4411 C CG1 . VAL B 192 ? 0.6272 0.3098 0.3370 -0.0480 -0.0293 0.0939  193 VAL B CG1 
4412 C CG2 . VAL B 192 ? 0.5845 0.3015 0.3098 -0.0466 -0.0313 0.0810  193 VAL B CG2 
4413 N N   . PRO B 193 ? 0.7736 0.3653 0.3770 -0.0614 0.0191  0.0999  194 PRO B N   
4414 C CA  . PRO B 193 ? 0.8205 0.3807 0.3919 -0.0626 0.0220  0.1056  194 PRO B CA  
4415 C C   . PRO B 193 ? 0.8116 0.3726 0.3929 -0.0588 -0.0014 0.1139  194 PRO B C   
4416 O O   . PRO B 193 ? 0.7631 0.3479 0.3809 -0.0558 -0.0143 0.1157  194 PRO B O   
4417 C CB  . PRO B 193 ? 0.8152 0.3735 0.3998 -0.0660 0.0541  0.1027  194 PRO B CB  
4418 C CG  . PRO B 193 ? 0.7687 0.3666 0.4072 -0.0648 0.0598  0.0962  194 PRO B CG  
4419 C CD  . PRO B 193 ? 0.7130 0.3340 0.3604 -0.0619 0.0430  0.0909  194 PRO B CD  
4420 N N   . LYS B 194 ? 0.8644 0.3974 0.4128 -0.0591 -0.0062 0.1188  195 LYS B N   
4421 C CA  . LYS B 194 ? 0.8586 0.3898 0.4143 -0.0555 -0.0292 0.1268  195 LYS B CA  
4422 C C   . LYS B 194 ? 0.8441 0.3922 0.4410 -0.0540 -0.0235 0.1303  195 LYS B C   
4423 O O   . LYS B 194 ? 0.8355 0.3989 0.4605 -0.0499 -0.0439 0.1342  195 LYS B O   
4424 C CB  . LYS B 194 ? 0.8478 0.3426 0.3588 -0.0570 -0.0311 0.1314  195 LYS B CB  
4425 C CG  . LYS B 194 ? 0.9733 0.4645 0.4935 -0.0536 -0.0515 0.1403  195 LYS B CG  
4426 C CD  . LYS B 194 ? 1.0039 0.4735 0.5112 -0.0554 -0.0345 0.1459  195 LYS B CD  
4427 C CE  . LYS B 194 ? 0.9544 0.4369 0.4980 -0.0517 -0.0452 0.1533  195 LYS B CE  
4428 N NZ  . LYS B 194 ? 1.0807 0.5417 0.6124 -0.0534 -0.0293 0.1592  195 LYS B NZ  
4429 N N   . THR B 195 ? 0.8073 0.3532 0.4116 -0.0574 0.0047  0.1280  196 THR B N   
4430 C CA  . THR B 195 ? 0.8461 0.4058 0.4898 -0.0569 0.0118  0.1298  196 THR B CA  
4431 C C   . THR B 195 ? 0.7514 0.3557 0.4485 -0.0535 0.0047  0.1218  196 THR B C   
4432 O O   . THR B 195 ? 0.7362 0.3635 0.4758 -0.0511 0.0060  0.1195  196 THR B O   
4433 C CB  . THR B 195 ? 0.8794 0.4315 0.5254 -0.0612 0.0445  0.1263  196 THR B CB  
4434 O OG1 . THR B 195 ? 0.9195 0.4780 0.5633 -0.0643 0.0627  0.1175  196 THR B OG1 
4435 C CG2 . THR B 195 ? 0.8819 0.4016 0.4896 -0.0625 0.0505  0.1318  196 THR B CG2 
4436 N N   . GLN B 196 ? 0.7044 0.3269 0.4047 -0.0522 -0.0027 0.1155  197 GLN B N   
4437 C CA  . GLN B 196 ? 0.7154 0.3843 0.4668 -0.0478 -0.0111 0.1065  197 GLN B CA  
4438 C C   . GLN B 196 ? 0.6870 0.3626 0.4412 -0.0435 -0.0404 0.1102  197 GLN B C   
4439 O O   . GLN B 196 ? 0.6063 0.3173 0.3986 -0.0398 -0.0477 0.1034  197 GLN B O   
4440 C CB  . GLN B 196 ? 0.6014 0.2906 0.3634 -0.0494 0.0043  0.0957  197 GLN B CB  
4441 C CG  . GLN B 196 ? 0.6402 0.3336 0.4179 -0.0528 0.0323  0.0897  197 GLN B CG  
4442 C CD  . GLN B 196 ? 0.6020 0.3285 0.4327 -0.0502 0.0345  0.0838  197 GLN B CD  
4443 O OE1 . GLN B 196 ? 0.5788 0.3346 0.4399 -0.0458 0.0196  0.0800  197 GLN B OE1 
4444 N NE2 . GLN B 196 ? 0.5623 0.2826 0.4035 -0.0532 0.0537  0.0827  197 GLN B NE2 
4445 N N   . MET B 197 ? 0.7008 0.3418 0.4160 -0.0439 -0.0574 0.1210  198 MET B N   
4446 C CA  . MET B 197 ? 0.7138 0.3586 0.4323 -0.0402 -0.0864 0.1246  198 MET B CA  
4447 C C   . MET B 197 ? 0.6467 0.3250 0.4207 -0.0348 -0.0979 0.1229  198 MET B C   
4448 O O   . MET B 197 ? 0.6332 0.3356 0.4331 -0.0314 -0.1114 0.1190  198 MET B O   
4449 C CB  . MET B 197 ? 0.8374 0.4519 0.5186 -0.0403 -0.1004 0.1312  198 MET B CB  
4450 C CG  . MET B 197 ? 0.9461 0.5619 0.6163 -0.0390 -0.1216 0.1285  198 MET B CG  
4451 S SD  . MET B 197 ? 1.2220 0.8168 0.8423 -0.0440 -0.1096 0.1226  198 MET B SD  
4452 C CE  . MET B 197 ? 0.8999 0.5272 0.5495 -0.0431 -0.1055 0.1153  198 MET B CE  
4453 N N   . GLN B 198 ? 0.6139 0.2928 0.4070 -0.0341 -0.0913 0.1255  199 GLN B N   
4454 C CA  . GLN B 198 ? 0.5910 0.2970 0.4343 -0.0292 -0.1010 0.1240  199 GLN B CA  
4455 C C   . GLN B 198 ? 0.5554 0.3046 0.4426 -0.0270 -0.0916 0.1113  199 GLN B C   
4456 O O   . GLN B 198 ? 0.5188 0.2907 0.4458 -0.0228 -0.1001 0.1091  199 GLN B O   
4457 C CB  . GLN B 198 ? 0.6178 0.3136 0.4706 -0.0294 -0.0936 0.1288  199 GLN B CB  
4458 C CG  . GLN B 198 ? 0.6302 0.3409 0.5000 -0.0319 -0.0663 0.1202  199 GLN B CG  
4459 C CD  . GLN B 198 ? 0.7346 0.4178 0.5625 -0.0376 -0.0474 0.1218  199 GLN B CD  
4460 O OE1 . GLN B 198 ? 0.7967 0.4498 0.5783 -0.0399 -0.0531 0.1282  199 GLN B OE1 
4461 N NE2 . GLN B 198 ? 0.7698 0.4615 0.6141 -0.0401 -0.0242 0.1156  199 GLN B NE2 
4462 N N   . ASN B 199 ? 0.5439 0.3033 0.4249 -0.0297 -0.0742 0.1030  200 ASN B N   
4463 C CA  . ASN B 199 ? 0.4654 0.2626 0.3836 -0.0279 -0.0654 0.0913  200 ASN B CA  
4464 C C   . ASN B 199 ? 0.4575 0.2688 0.3757 -0.0264 -0.0745 0.0875  200 ASN B C   
4465 O O   . ASN B 199 ? 0.3767 0.2176 0.3230 -0.0245 -0.0694 0.0787  200 ASN B O   
4466 C CB  . ASN B 199 ? 0.4416 0.2437 0.3604 -0.0316 -0.0413 0.0842  200 ASN B CB  
4467 C CG  . ASN B 199 ? 0.5163 0.3094 0.4436 -0.0331 -0.0304 0.0862  200 ASN B CG  
4468 O OD1 . ASN B 199 ? 0.5215 0.3204 0.4719 -0.0303 -0.0381 0.0882  200 ASN B OD1 
4469 N ND2 . ASN B 199 ? 0.4789 0.2574 0.3896 -0.0376 -0.0114 0.0853  200 ASN B ND2 
4470 N N   . TYR B 200 ? 0.4718 0.2612 0.3584 -0.0271 -0.0886 0.0941  201 TYR B N   
4471 C CA  . TYR B 200 ? 0.4691 0.2681 0.3517 -0.0264 -0.0961 0.0906  201 TYR B CA  
4472 C C   . TYR B 200 ? 0.4617 0.2810 0.3787 -0.0214 -0.1138 0.0906  201 TYR B C   
4473 O O   . TYR B 200 ? 0.5443 0.3515 0.4646 -0.0195 -0.1310 0.0982  201 TYR B O   
4474 C CB  . TYR B 200 ? 0.5004 0.2642 0.3330 -0.0296 -0.1042 0.0972  201 TYR B CB  
4475 C CG  . TYR B 200 ? 0.5858 0.3538 0.4065 -0.0301 -0.1090 0.0932  201 TYR B CG  
4476 C CD1 . TYR B 200 ? 0.6205 0.3988 0.4572 -0.0269 -0.1297 0.0941  201 TYR B CD1 
4477 C CD2 . TYR B 200 ? 0.6221 0.3818 0.4165 -0.0340 -0.0924 0.0888  201 TYR B CD2 
4478 C CE1 . TYR B 200 ? 0.6347 0.4157 0.4607 -0.0276 -0.1340 0.0905  201 TYR B CE1 
4479 C CE2 . TYR B 200 ? 0.6398 0.4019 0.4230 -0.0346 -0.0964 0.0851  201 TYR B CE2 
4480 C CZ  . TYR B 200 ? 0.6026 0.3753 0.4007 -0.0314 -0.1173 0.0860  201 TYR B CZ  
4481 O OH  . TYR B 200 ? 0.6054 0.3795 0.3926 -0.0322 -0.1209 0.0822  201 TYR B OH  
4482 N N   . ALA B 201 ? 0.4332 0.2820 0.3764 -0.0194 -0.1094 0.0823  202 ALA B N   
4483 C CA  . ALA B 201 ? 0.4072 0.2771 0.3868 -0.0148 -0.1213 0.0810  202 ALA B CA  
4484 C C   . ALA B 201 ? 0.4791 0.3412 0.4476 -0.0143 -0.1392 0.0844  202 ALA B C   
4485 O O   . ALA B 201 ? 0.3997 0.2663 0.3557 -0.0157 -0.1355 0.0802  202 ALA B O   
4486 C CB  . ALA B 201 ? 0.3637 0.2655 0.3728 -0.0130 -0.1076 0.0709  202 ALA B CB  
4487 N N   . PHE B 202 ? 0.4464 0.2971 0.4224 -0.0123 -0.1594 0.0918  203 PHE B N   
4488 C CA  . PHE B 202 ? 0.4764 0.3213 0.4481 -0.0119 -0.1780 0.0940  203 PHE B CA  
4489 C C   . PHE B 202 ? 0.5012 0.3751 0.5191 -0.0084 -0.1802 0.0881  203 PHE B C   
4490 O O   . PHE B 202 ? 0.4860 0.3626 0.5046 -0.0094 -0.1864 0.0845  203 PHE B O   
4491 C CB  . PHE B 202 ? 0.4806 0.3032 0.4379 -0.0138 -0.1916 0.0980  203 PHE B CB  
4492 C CG  . PHE B 202 ? 0.6116 0.4015 0.5170 -0.0179 -0.1895 0.1027  203 PHE B CG  
4493 C CD1 . PHE B 202 ? 0.6740 0.4473 0.5410 -0.0215 -0.1904 0.1007  203 PHE B CD1 
4494 C CD2 . PHE B 202 ? 0.6011 0.3753 0.4961 -0.0183 -0.1852 0.1088  203 PHE B CD2 
4495 C CE1 . PHE B 202 ? 0.7129 0.4541 0.5307 -0.0255 -0.1859 0.1042  203 PHE B CE1 
4496 C CE2 . PHE B 202 ? 0.6833 0.4258 0.5295 -0.0224 -0.1803 0.1128  203 PHE B CE2 
4497 C CZ  . PHE B 202 ? 0.7302 0.4561 0.5373 -0.0260 -0.1802 0.1103  203 PHE B CZ  
4498 N N   . GLY B 203 ? 0.4183 0.3115 0.4740 -0.0047 -0.1740 0.0867  204 GLY B N   
4499 C CA  . GLY B 203 ? 0.3487 0.2663 0.4455 -0.0019 -0.1723 0.0807  204 GLY B CA  
4500 C C   . GLY B 203 ? 0.4230 0.3340 0.5344 -0.0030 -0.1850 0.0815  204 GLY B C   
4501 O O   . GLY B 203 ? 0.3988 0.2963 0.5099 -0.0037 -0.1932 0.0862  204 GLY B O   
4502 N N   . TYR B 204 ? 0.4024 0.3223 0.5279 -0.0033 -0.1871 0.0772  205 TYR B N   
4503 C CA  . TYR B 204 ? 0.3970 0.3084 0.5360 -0.0051 -0.2007 0.0781  205 TYR B CA  
4504 C C   . TYR B 204 ? 0.4639 0.3498 0.5644 -0.0089 -0.2152 0.0815  205 TYR B C   
4505 O O   . TYR B 204 ? 0.5329 0.4067 0.6399 -0.0107 -0.2298 0.0836  205 TYR B O   
4506 C CB  . TYR B 204 ? 0.4081 0.3341 0.5737 -0.0045 -0.1977 0.0730  205 TYR B CB  
4507 C CG  . TYR B 204 ? 0.3699 0.3165 0.5762 -0.0013 -0.1847 0.0695  205 TYR B CG  
4508 C CD1 . TYR B 204 ? 0.4216 0.3688 0.6614 -0.0010 -0.1879 0.0707  205 TYR B CD1 
4509 C CD2 . TYR B 204 ? 0.3689 0.3333 0.5796 0.0012  -0.1690 0.0649  205 TYR B CD2 
4510 C CE1 . TYR B 204 ? 0.4309 0.3944 0.7061 0.0016  -0.1741 0.0671  205 TYR B CE1 
4511 C CE2 . TYR B 204 ? 0.3554 0.3357 0.5991 0.0040  -0.1560 0.0613  205 TYR B CE2 
4512 C CZ  . TYR B 204 ? 0.4067 0.3858 0.6820 0.0042  -0.1579 0.0623  205 TYR B CZ  
4513 O OH  . TYR B 204 ? 0.4045 0.3969 0.7106 0.0067  -0.1433 0.0583  205 TYR B OH  
4514 N N   . ASN B 205 ? 0.5069 0.3832 0.5677 -0.0104 -0.2114 0.0818  206 ASN B N   
4515 C CA  . ASN B 205 ? 0.5661 0.4160 0.5849 -0.0142 -0.2221 0.0839  206 ASN B CA  
4516 C C   . ASN B 205 ? 0.6360 0.4817 0.6661 -0.0159 -0.2355 0.0816  206 ASN B C   
4517 O O   . ASN B 205 ? 0.6147 0.4401 0.6345 -0.0183 -0.2512 0.0844  206 ASN B O   
4518 C CB  . ASN B 205 ? 0.5804 0.4069 0.5747 -0.0157 -0.2290 0.0903  206 ASN B CB  
4519 C CG  . ASN B 205 ? 0.7016 0.4983 0.6426 -0.0198 -0.2341 0.0921  206 ASN B CG  
4520 O OD1 . ASN B 205 ? 0.6925 0.4874 0.6120 -0.0213 -0.2285 0.0886  206 ASN B OD1 
4521 N ND2 . ASN B 205 ? 0.6786 0.4506 0.5971 -0.0217 -0.2439 0.0973  206 ASN B ND2 
4522 N N   . GLN B 206 ? 0.5796 0.4440 0.6318 -0.0145 -0.2292 0.0765  207 GLN B N   
4523 C CA  . GLN B 206 ? 0.5865 0.4503 0.6595 -0.0156 -0.2399 0.0744  207 GLN B CA  
4524 C C   . GLN B 206 ? 0.6732 0.5108 0.7108 -0.0194 -0.2542 0.0750  207 GLN B C   
4525 O O   . GLN B 206 ? 0.6966 0.5256 0.7480 -0.0210 -0.2689 0.0750  207 GLN B O   
4526 C CB  . GLN B 206 ? 0.5534 0.4404 0.6520 -0.0133 -0.2278 0.0693  207 GLN B CB  
4527 C CG  . GLN B 206 ? 0.5575 0.4488 0.6292 -0.0132 -0.2171 0.0665  207 GLN B CG  
4528 C CD  . GLN B 206 ? 0.5529 0.4661 0.6504 -0.0109 -0.2064 0.0617  207 GLN B CD  
4529 O OE1 . GLN B 206 ? 0.5020 0.4190 0.6277 -0.0107 -0.2109 0.0604  207 GLN B OE1 
4530 N NE2 . GLN B 206 ? 0.4998 0.4265 0.5884 -0.0094 -0.1922 0.0594  207 GLN B NE2 
4531 N N   . GLU B 207 ? 0.6889 0.5121 0.6814 -0.0212 -0.2504 0.0754  208 GLU B N   
4532 C CA  . GLU B 207 ? 0.7636 0.5583 0.7173 -0.0251 -0.2627 0.0757  208 GLU B CA  
4533 C C   . GLU B 207 ? 0.8022 0.5693 0.7298 -0.0275 -0.2754 0.0809  208 GLU B C   
4534 O O   . GLU B 207 ? 0.8159 0.5551 0.7080 -0.0310 -0.2868 0.0814  208 GLU B O   
4535 C CB  . GLU B 207 ? 0.7378 0.5271 0.6536 -0.0264 -0.2509 0.0731  208 GLU B CB  
4536 C CG  . GLU B 207 ? 0.6610 0.4789 0.5999 -0.0237 -0.2362 0.0686  208 GLU B CG  
4537 C CD  . GLU B 207 ? 0.7101 0.5391 0.6794 -0.0229 -0.2419 0.0650  208 GLU B CD  
4538 O OE1 . GLU B 207 ? 0.7613 0.5733 0.7293 -0.0249 -0.2582 0.0655  208 GLU B OE1 
4539 O OE2 . GLU B 207 ? 0.7013 0.5549 0.6954 -0.0202 -0.2300 0.0618  208 GLU B OE2 
4540 N N   . ASN B 208 ? 0.7701 0.5434 0.7140 -0.0257 -0.2737 0.0848  209 ASN B N   
4541 C CA  . ASN B 208 ? 0.8214 0.5701 0.7426 -0.0275 -0.2845 0.0905  209 ASN B CA  
4542 C C   . ASN B 208 ? 0.8862 0.6051 0.7465 -0.0308 -0.2819 0.0918  209 ASN B C   
4543 O O   . ASN B 208 ? 0.9425 0.6318 0.7718 -0.0341 -0.2961 0.0935  209 ASN B O   
4544 C CB  . ASN B 208 ? 0.8429 0.5804 0.7827 -0.0291 -0.3067 0.0919  209 ASN B CB  
4545 C CG  . ASN B 208 ? 0.9115 0.6753 0.9119 -0.0263 -0.3073 0.0910  209 ASN B CG  
4546 O OD1 . ASN B 208 ? 0.9871 0.7562 1.0076 -0.0248 -0.3075 0.0946  209 ASN B OD1 
4547 N ND2 . ASN B 208 ? 0.9163 0.6954 0.9459 -0.0257 -0.3065 0.0864  209 ASN B ND2 
4548 N N   . GLN B 209 ? 0.8906 0.6162 0.7337 -0.0301 -0.2627 0.0910  210 GLN B N   
4549 C CA  . GLN B 209 ? 0.9358 0.6346 0.7231 -0.0335 -0.2549 0.0914  210 GLN B CA  
4550 C C   . GLN B 209 ? 0.9331 0.6257 0.7024 -0.0330 -0.2409 0.0961  210 GLN B C   
4551 O O   . GLN B 209 ? 0.8600 0.5754 0.6619 -0.0296 -0.2334 0.0977  210 GLN B O   
4552 C CB  . GLN B 209 ? 0.9163 0.6236 0.6942 -0.0341 -0.2428 0.0856  210 GLN B CB  
4553 C CG  . GLN B 209 ? 0.9528 0.6566 0.7344 -0.0355 -0.2554 0.0813  210 GLN B CG  
4554 C CD  . GLN B 209 ? 1.0710 0.7666 0.8213 -0.0378 -0.2451 0.0767  210 GLN B CD  
4555 O OE1 . GLN B 209 ? 1.0117 0.7304 0.7775 -0.0360 -0.2316 0.0735  210 GLN B OE1 
4556 N NE2 . GLN B 209 ? 1.1282 0.7893 0.8334 -0.0420 -0.2514 0.0763  210 GLN B NE2 
4557 N N   . PRO B 210 ? 0.9784 0.6384 0.6958 -0.0366 -0.2362 0.0983  211 PRO B N   
4558 C CA  . PRO B 210 ? 1.0340 0.6863 0.7324 -0.0368 -0.2189 0.1026  211 PRO B CA  
4559 C C   . PRO B 210 ? 1.0343 0.6928 0.7193 -0.0378 -0.1968 0.0990  211 PRO B C   
4560 O O   . PRO B 210 ? 0.9902 0.6751 0.7027 -0.0360 -0.1937 0.0945  211 PRO B O   
4561 C CB  . PRO B 210 ? 1.0506 0.6622 0.6993 -0.0405 -0.2237 0.1062  211 PRO B CB  
4562 C CG  . PRO B 210 ? 1.0989 0.6944 0.7243 -0.0436 -0.2341 0.1013  211 PRO B CG  
4563 C CD  . PRO B 210 ? 1.0466 0.6724 0.7209 -0.0409 -0.2468 0.0974  211 PRO B CD  
4564 N N   . ILE B 211 ? 1.1412 0.7748 0.7846 -0.0411 -0.1804 0.1007  212 ILE B N   
4565 C CA  . ILE B 211 ? 1.1665 0.8028 0.7962 -0.0430 -0.1576 0.0972  212 ILE B CA  
4566 C C   . ILE B 211 ? 1.2077 0.8083 0.7828 -0.0482 -0.1470 0.0948  212 ILE B C   
4567 O O   . ILE B 211 ? 1.2692 0.8624 0.8287 -0.0500 -0.1518 0.0897  212 ILE B O   
4568 C CB  . ILE B 211 ? 1.1098 0.7560 0.7543 -0.0421 -0.1399 0.1009  212 ILE B CB  
4569 C CG1 . ILE B 211 ? 1.0527 0.7294 0.7492 -0.0370 -0.1515 0.1034  212 ILE B CG1 
4570 C CG2 . ILE B 211 ? 1.0580 0.7110 0.6976 -0.0443 -0.1171 0.0969  212 ILE B CG2 
4571 C CD1 . ILE B 211 ? 1.0015 0.6845 0.7132 -0.0364 -0.1367 0.1071  212 ILE B CD1 
4572 N N   . GLY B 216 ? 0.9128 0.5355 0.4506 -0.0582 -0.1223 0.0466  217 GLY B N   
4573 C CA  . GLY B 216 ? 0.8669 0.4989 0.4127 -0.0582 -0.1251 0.0411  217 GLY B CA  
4574 C C   . GLY B 216 ? 0.8113 0.4242 0.3248 -0.0625 -0.1025 0.0352  217 GLY B C   
4575 O O   . GLY B 216 ? 0.8184 0.4178 0.3116 -0.0650 -0.0804 0.0349  217 GLY B O   
4576 N N   . PRO B 217 ? 0.8597 0.4714 0.3708 -0.0635 -0.1065 0.0301  218 PRO B N   
4577 C CA  . PRO B 217 ? 0.8250 0.4184 0.3077 -0.0676 -0.0839 0.0237  218 PRO B CA  
4578 C C   . PRO B 217 ? 0.7345 0.3517 0.2369 -0.0670 -0.0608 0.0213  218 PRO B C   
4579 O O   . PRO B 217 ? 0.7647 0.4159 0.3035 -0.0635 -0.0666 0.0212  218 PRO B O   
4580 C CB  . PRO B 217 ? 0.8615 0.4554 0.3472 -0.0677 -0.0975 0.0195  218 PRO B CB  
4581 C CG  . PRO B 217 ? 0.8252 0.4534 0.3573 -0.0625 -0.1206 0.0228  218 PRO B CG  
4582 C CD  . PRO B 217 ? 0.8565 0.4863 0.3965 -0.0605 -0.1296 0.0297  218 PRO B CD  
4583 N N   . LEU B 218 ? 0.7634 0.3618 0.2433 -0.0704 -0.0338 0.0194  219 LEU B N   
4584 C CA  . LEU B 218 ? 0.7615 0.3787 0.2606 -0.0705 -0.0081 0.0172  219 LEU B CA  
4585 C C   . LEU B 218 ? 0.7368 0.3970 0.2891 -0.0647 -0.0174 0.0212  219 LEU B C   
4586 O O   . LEU B 218 ? 0.6686 0.3661 0.2688 -0.0613 -0.0092 0.0173  219 LEU B O   
4587 C CB  . LEU B 218 ? 0.7297 0.3585 0.2428 -0.0710 0.0058  0.0088  219 LEU B CB  
4588 C CG  . LEU B 218 ? 0.7865 0.3792 0.2608 -0.0762 0.0238  0.0026  219 LEU B CG  
4589 C CD1 . LEU B 218 ? 0.7943 0.4035 0.2903 -0.0763 0.0410  -0.0055 219 LEU B CD1 
4590 C CD2 . LEU B 218 ? 0.8354 0.4015 0.2884 -0.0794 0.0471  0.0031  219 LEU B CD2 
4591 N N   . GLY B 219 ? 0.6908 0.3457 0.2372 -0.0635 -0.0347 0.0287  220 GLY B N   
4592 C CA  . GLY B 219 ? 0.6501 0.3440 0.2468 -0.0578 -0.0477 0.0319  220 GLY B CA  
4593 C C   . GLY B 219 ? 0.6642 0.3814 0.2943 -0.0560 -0.0289 0.0317  220 GLY B C   
4594 O O   . GLY B 219 ? 0.6178 0.3738 0.2964 -0.0513 -0.0313 0.0304  220 GLY B O   
4595 N N   . ALA B 220 ? 0.6601 0.3524 0.2640 -0.0597 -0.0100 0.0328  221 ALA B N   
4596 C CA  . ALA B 220 ? 0.6351 0.3461 0.2699 -0.0585 0.0066  0.0328  221 ALA B CA  
4597 C C   . ALA B 220 ? 0.5831 0.3324 0.2676 -0.0557 0.0198  0.0260  221 ALA B C   
4598 O O   . ALA B 220 ? 0.5522 0.3327 0.2776 -0.0518 0.0166  0.0265  221 ALA B O   
4599 C CB  . ALA B 220 ? 0.6576 0.3316 0.2541 -0.0638 0.0284  0.0341  221 ALA B CB  
4600 N N   . PRO B 221 ? 0.5954 0.3439 0.2795 -0.0573 0.0336  0.0197  222 PRO B N   
4601 C CA  . PRO B 221 ? 0.5398 0.3254 0.2738 -0.0542 0.0428  0.0141  222 PRO B CA  
4602 C C   . PRO B 221 ? 0.4901 0.3102 0.2583 -0.0486 0.0224  0.0146  222 PRO B C   
4603 O O   . PRO B 221 ? 0.4731 0.3247 0.2829 -0.0453 0.0263  0.0118  222 PRO B O   
4604 C CB  . PRO B 221 ? 0.5757 0.3472 0.2963 -0.0573 0.0598  0.0080  222 PRO B CB  
4605 C CG  . PRO B 221 ? 0.6373 0.3610 0.2988 -0.0630 0.0663  0.0098  222 PRO B CG  
4606 C CD  . PRO B 221 ? 0.6522 0.3648 0.2905 -0.0622 0.0415  0.0171  222 PRO B CD  
4607 N N   . ALA B 222 ? 0.4542 0.2680 0.2067 -0.0477 0.0009  0.0180  223 ALA B N   
4608 C CA  . ALA B 222 ? 0.4912 0.3354 0.2766 -0.0427 -0.0161 0.0184  223 ALA B CA  
4609 C C   . ALA B 222 ? 0.4722 0.3327 0.2787 -0.0392 -0.0287 0.0231  223 ALA B C   
4610 O O   . ALA B 222 ? 0.4362 0.3278 0.2802 -0.0350 -0.0317 0.0220  223 ALA B O   
4611 C CB  . ALA B 222 ? 0.4772 0.3081 0.2418 -0.0434 -0.0325 0.0188  223 ALA B CB  
4612 N N   . TYR B 223 ? 0.4824 0.3211 0.2648 -0.0409 -0.0355 0.0284  224 TYR B N   
4613 C CA  . TYR B 223 ? 0.4614 0.3145 0.2652 -0.0375 -0.0484 0.0329  224 TYR B CA  
4614 C C   . TYR B 223 ? 0.4792 0.3096 0.2610 -0.0397 -0.0477 0.0381  224 TYR B C   
4615 O O   . TYR B 223 ? 0.5136 0.3456 0.3025 -0.0375 -0.0629 0.0431  224 TYR B O   
4616 C CB  . TYR B 223 ? 0.4638 0.3218 0.2742 -0.0349 -0.0715 0.0357  224 TYR B CB  
4617 C CG  . TYR B 223 ? 0.5295 0.3570 0.3011 -0.0383 -0.0827 0.0371  224 TYR B CG  
4618 C CD1 . TYR B 223 ? 0.5810 0.3757 0.3158 -0.0411 -0.0919 0.0425  224 TYR B CD1 
4619 C CD2 . TYR B 223 ? 0.5320 0.3621 0.3029 -0.0386 -0.0852 0.0330  224 TYR B CD2 
4620 C CE1 . TYR B 223 ? 0.6408 0.4044 0.3363 -0.0444 -0.1043 0.0436  224 TYR B CE1 
4621 C CE2 . TYR B 223 ? 0.5802 0.3810 0.3146 -0.0419 -0.0966 0.0335  224 TYR B CE2 
4622 C CZ  . TYR B 223 ? 0.6131 0.3801 0.3087 -0.0449 -0.1067 0.0386  224 TYR B CZ  
4623 O OH  . TYR B 223 ? 0.6920 0.4271 0.3484 -0.0484 -0.1194 0.0387  224 TYR B OH  
4624 N N   . GLY B 224 ? 0.4960 0.3058 0.2546 -0.0438 -0.0292 0.0371  225 GLY B N   
4625 C CA  . GLY B 224 ? 0.5158 0.2964 0.2445 -0.0466 -0.0278 0.0427  225 GLY B CA  
4626 C C   . GLY B 224 ? 0.4890 0.2788 0.2380 -0.0460 -0.0175 0.0440  225 GLY B C   
4627 O O   . GLY B 224 ? 0.5432 0.3061 0.2652 -0.0485 -0.0151 0.0492  225 GLY B O   
4628 N N   . VAL B 225 ? 0.4525 0.2772 0.2461 -0.0428 -0.0118 0.0396  226 VAL B N   
4629 C CA  . VAL B 225 ? 0.3970 0.2302 0.2111 -0.0428 0.0003  0.0390  226 VAL B CA  
4630 C C   . VAL B 225 ? 0.4129 0.2627 0.2507 -0.0389 -0.0149 0.0423  226 VAL B C   
4631 O O   . VAL B 225 ? 0.4085 0.2790 0.2666 -0.0350 -0.0292 0.0417  226 VAL B O   
4632 C CB  . VAL B 225 ? 0.4261 0.2837 0.2731 -0.0424 0.0168  0.0313  226 VAL B CB  
4633 C CG1 . VAL B 225 ? 0.4268 0.2906 0.2950 -0.0431 0.0287  0.0302  226 VAL B CG1 
4634 C CG2 . VAL B 225 ? 0.4592 0.3015 0.2880 -0.0460 0.0329  0.0276  226 VAL B CG2 
4635 N N   . LYS B 226 ? 0.4308 0.2703 0.2667 -0.0400 -0.0105 0.0457  227 LYS B N   
4636 C CA  . LYS B 226 ? 0.4131 0.2669 0.2736 -0.0367 -0.0206 0.0481  227 LYS B CA  
4637 C C   . LYS B 226 ? 0.3965 0.2626 0.2820 -0.0373 -0.0049 0.0441  227 LYS B C   
4638 O O   . LYS B 226 ? 0.4101 0.2619 0.2845 -0.0412 0.0126  0.0429  227 LYS B O   
4639 C CB  . LYS B 226 ? 0.4500 0.2765 0.2840 -0.0373 -0.0336 0.0572  227 LYS B CB  
4640 C CG  . LYS B 226 ? 0.4662 0.2764 0.2735 -0.0372 -0.0517 0.0615  227 LYS B CG  
4641 C CD  . LYS B 226 ? 0.5434 0.3188 0.3029 -0.0422 -0.0434 0.0629  227 LYS B CD  
4642 C CE  . LYS B 226 ? 0.6154 0.3739 0.3478 -0.0425 -0.0628 0.0660  227 LYS B CE  
4643 N NZ  . LYS B 226 ? 0.6366 0.3565 0.3165 -0.0477 -0.0544 0.0672  227 LYS B NZ  
4644 N N   . SER B 227 ? 0.3823 0.2738 0.3021 -0.0338 -0.0104 0.0414  228 SER B N   
4645 C CA  . SER B 227 ? 0.3413 0.2465 0.2874 -0.0344 0.0027  0.0361  228 SER B CA  
4646 C C   . SER B 227 ? 0.3426 0.2642 0.3150 -0.0310 -0.0059 0.0356  228 SER B C   
4647 O O   . SER B 227 ? 0.3175 0.2427 0.2920 -0.0279 -0.0206 0.0390  228 SER B O   
4648 C CB  . SER B 227 ? 0.3619 0.2874 0.3274 -0.0342 0.0113  0.0281  228 SER B CB  
4649 O OG  . SER B 227 ? 0.3600 0.2951 0.3498 -0.0356 0.0237  0.0228  228 SER B OG  
4650 N N   . THR B 228 ? 0.3430 0.2742 0.3376 -0.0318 0.0040  0.0309  229 THR B N   
4651 C CA  . THR B 228 ? 0.3017 0.2475 0.3219 -0.0293 -0.0010 0.0286  229 THR B CA  
4652 C C   . THR B 228 ? 0.2987 0.2718 0.3461 -0.0272 -0.0008 0.0197  229 THR B C   
4653 O O   . THR B 228 ? 0.3020 0.2822 0.3525 -0.0282 0.0053  0.0154  229 THR B O   
4654 C CB  . THR B 228 ? 0.3145 0.2491 0.3396 -0.0320 0.0088  0.0294  229 THR B CB  
4655 O OG1 . THR B 228 ? 0.2751 0.2142 0.3126 -0.0350 0.0238  0.0232  229 THR B OG1 
4656 C CG2 . THR B 228 ? 0.3350 0.2386 0.3289 -0.0343 0.0091  0.0391  229 THR B CG2 
4657 N N   . LEU B 229 ? 0.2450 0.2318 0.3113 -0.0242 -0.0075 0.0171  230 LEU B N   
4658 C CA  . LEU B 229 ? 0.2308 0.2396 0.3185 -0.0224 -0.0078 0.0086  230 LEU B CA  
4659 C C   . LEU B 229 ? 0.2612 0.2739 0.3631 -0.0253 0.0025  0.0023  230 LEU B C   
4660 O O   . LEU B 229 ? 0.2348 0.2599 0.3454 -0.0250 0.0032  -0.0029 230 LEU B O   
4661 C CB  . LEU B 229 ? 0.2213 0.2393 0.3235 -0.0192 -0.0145 0.0064  230 LEU B CB  
4662 C CG  . LEU B 229 ? 0.2325 0.2694 0.3502 -0.0173 -0.0158 -0.0022 230 LEU B CG  
4663 C CD1 . LEU B 229 ? 0.2172 0.2628 0.3280 -0.0154 -0.0197 -0.0023 230 LEU B CD1 
4664 C CD2 . LEU B 229 ? 0.2311 0.2734 0.3604 -0.0147 -0.0196 -0.0052 230 LEU B CD2 
4665 N N   . PRO B 230 ? 0.2796 0.2827 0.3875 -0.0282 0.0102  0.0023  231 PRO B N   
4666 C CA  . PRO B 230 ? 0.2627 0.2706 0.3894 -0.0311 0.0198  -0.0042 231 PRO B CA  
4667 C C   . PRO B 230 ? 0.2696 0.2732 0.3904 -0.0335 0.0287  -0.0040 231 PRO B C   
4668 O O   . PRO B 230 ? 0.2436 0.2596 0.3846 -0.0341 0.0316  -0.0106 231 PRO B O   
4669 C CB  . PRO B 230 ? 0.3156 0.3097 0.4463 -0.0339 0.0275  -0.0022 231 PRO B CB  
4670 C CG  . PRO B 230 ? 0.3067 0.2975 0.4304 -0.0311 0.0182  0.0022  231 PRO B CG  
4671 C CD  . PRO B 230 ? 0.2793 0.2684 0.3823 -0.0286 0.0098  0.0077  231 PRO B CD  
4672 N N   . ASP B 231 ? 0.2695 0.2547 0.3634 -0.0348 0.0328  0.0032  232 ASP B N   
4673 C CA  . ASP B 231 ? 0.2922 0.2715 0.3785 -0.0371 0.0425  0.0030  232 ASP B CA  
4674 C C   . ASP B 231 ? 0.2806 0.2778 0.3726 -0.0341 0.0346  -0.0005 232 ASP B C   
4675 O O   . ASP B 231 ? 0.3084 0.3125 0.4144 -0.0352 0.0412  -0.0051 232 ASP B O   
4676 C CB  . ASP B 231 ? 0.3293 0.2818 0.3794 -0.0392 0.0473  0.0112  232 ASP B CB  
4677 C CG  . ASP B 231 ? 0.3881 0.3181 0.4312 -0.0438 0.0635  0.0139  232 ASP B CG  
4678 O OD1 . ASP B 231 ? 0.3787 0.3150 0.4470 -0.0449 0.0690  0.0101  232 ASP B OD1 
4679 O OD2 . ASP B 231 ? 0.4233 0.3277 0.4346 -0.0464 0.0710  0.0196  232 ASP B OD2 
4680 N N   . MET B 232 ? 0.2544 0.2585 0.3373 -0.0304 0.0210  0.0018  233 MET B N   
4681 C CA  . MET B 232 ? 0.2392 0.2586 0.3263 -0.0276 0.0143  -0.0009 233 MET B CA  
4682 C C   . MET B 232 ? 0.2428 0.2825 0.3576 -0.0261 0.0113  -0.0086 233 MET B C   
4683 O O   . MET B 232 ? 0.2384 0.2882 0.3616 -0.0253 0.0106  -0.0117 233 MET B O   
4684 C CB  . MET B 232 ? 0.2156 0.2364 0.2887 -0.0242 0.0018  0.0034  233 MET B CB  
4685 C CG  . MET B 232 ? 0.2584 0.2593 0.3030 -0.0256 0.0012  0.0107  233 MET B CG  
4686 S SD  . MET B 232 ? 0.2932 0.2834 0.3228 -0.0286 0.0116  0.0105  233 MET B SD  
4687 C CE  . MET B 232 ? 0.2778 0.2904 0.3202 -0.0248 0.0038  0.0067  233 MET B CE  
4688 N N   . LEU B 233 ? 0.1978 0.2421 0.3263 -0.0259 0.0087  -0.0118 234 LEU B N   
4689 C CA  . LEU B 233 ? 0.2252 0.2851 0.3777 -0.0252 0.0049  -0.0197 234 LEU B CA  
4690 C C   . LEU B 233 ? 0.2124 0.2725 0.3845 -0.0285 0.0145  -0.0236 234 LEU B C   
4691 O O   . LEU B 233 ? 0.2210 0.2938 0.4114 -0.0276 0.0102  -0.0290 234 LEU B O   
4692 C CB  . LEU B 233 ? 0.2139 0.2762 0.3753 -0.0246 0.0005  -0.0230 234 LEU B CB  
4693 C CG  . LEU B 233 ? 0.2244 0.2894 0.3739 -0.0209 -0.0085 -0.0210 234 LEU B CG  
4694 C CD1 . LEU B 233 ? 0.2486 0.3131 0.4072 -0.0209 -0.0102 -0.0246 234 LEU B CD1 
4695 C CD2 . LEU B 233 ? 0.2395 0.3168 0.3880 -0.0177 -0.0165 -0.0238 234 LEU B CD2 
4696 N N   . SER B 234 ? 0.1852 0.2302 0.3546 -0.0322 0.0275  -0.0209 235 SER B N   
4697 C CA  . SER B 234 ? 0.2128 0.2561 0.4021 -0.0356 0.0399  -0.0242 235 SER B CA  
4698 C C   . SER B 234 ? 0.2256 0.2710 0.4110 -0.0350 0.0426  -0.0235 235 SER B C   
4699 O O   . SER B 234 ? 0.1908 0.2452 0.4019 -0.0357 0.0454  -0.0285 235 SER B O   
4700 C CB  . SER B 234 ? 0.2233 0.2459 0.4051 -0.0399 0.0560  -0.0204 235 SER B CB  
4701 O OG  . SER B 234 ? 0.3164 0.3378 0.5096 -0.0409 0.0557  -0.0220 235 SER B OG  
4702 N N   . PHE B 235 ? 0.2248 0.2611 0.3799 -0.0339 0.0414  -0.0175 236 PHE B N   
4703 C CA  . PHE B 235 ? 0.1944 0.2327 0.3447 -0.0332 0.0431  -0.0172 236 PHE B CA  
4704 C C   . PHE B 235 ? 0.2400 0.2998 0.4088 -0.0294 0.0302  -0.0215 236 PHE B C   
4705 O O   . PHE B 235 ? 0.2509 0.3171 0.4348 -0.0294 0.0330  -0.0241 236 PHE B O   
4706 C CB  . PHE B 235 ? 0.2256 0.2507 0.3400 -0.0325 0.0408  -0.0104 236 PHE B CB  
4707 C CG  . PHE B 235 ? 0.2490 0.2735 0.3561 -0.0322 0.0436  -0.0101 236 PHE B CG  
4708 C CD1 . PHE B 235 ? 0.2580 0.2752 0.3737 -0.0353 0.0591  -0.0125 236 PHE B CD1 
4709 C CD2 . PHE B 235 ? 0.2600 0.2900 0.3528 -0.0289 0.0319  -0.0076 236 PHE B CD2 
4710 C CE1 . PHE B 235 ? 0.3043 0.3201 0.4143 -0.0350 0.0626  -0.0127 236 PHE B CE1 
4711 C CE2 . PHE B 235 ? 0.3054 0.3343 0.3923 -0.0287 0.0345  -0.0076 236 PHE B CE2 
4712 C CZ  . PHE B 235 ? 0.2838 0.3056 0.3787 -0.0318 0.0498  -0.0103 236 PHE B CZ  
4713 N N   . ILE B 236 ? 0.2183 0.2879 0.3853 -0.0263 0.0166  -0.0221 237 ILE B N   
4714 C CA  . ILE B 236 ? 0.2111 0.2973 0.3903 -0.0229 0.0044  -0.0258 237 ILE B CA  
4715 C C   . ILE B 236 ? 0.2134 0.3087 0.4251 -0.0241 0.0036  -0.0326 237 ILE B C   
4716 O O   . ILE B 236 ? 0.1601 0.2655 0.3866 -0.0224 -0.0023 -0.0353 237 ILE B O   
4717 C CB  . ILE B 236 ? 0.2123 0.3033 0.3794 -0.0196 -0.0076 -0.0252 237 ILE B CB  
4718 C CG1 . ILE B 236 ? 0.1978 0.2824 0.3391 -0.0179 -0.0088 -0.0186 237 ILE B CG1 
4719 C CG2 . ILE B 236 ? 0.2257 0.3304 0.4038 -0.0166 -0.0195 -0.0298 237 ILE B CG2 
4720 C CD1 . ILE B 236 ? 0.2379 0.3236 0.3729 -0.0171 -0.0078 -0.0163 237 ILE B CD1 
4721 N N   . HIS B 237 ? 0.1969 0.2882 0.4217 -0.0269 0.0086  -0.0354 238 HIS B N   
4722 C CA  . HIS B 237 ? 0.2180 0.3170 0.4779 -0.0285 0.0076  -0.0423 238 HIS B CA  
4723 C C   . HIS B 237 ? 0.2207 0.3198 0.5009 -0.0303 0.0181  -0.0431 238 HIS B C   
4724 O O   . HIS B 237 ? 0.1982 0.3083 0.5078 -0.0298 0.0117  -0.0480 238 HIS B O   
4725 C CB  . HIS B 237 ? 0.2274 0.3201 0.4982 -0.0318 0.0138  -0.0446 238 HIS B CB  
4726 C CG  . HIS B 237 ? 0.2159 0.3149 0.5268 -0.0342 0.0149  -0.0517 238 HIS B CG  
4727 N ND1 . HIS B 237 ? 0.2854 0.3769 0.6167 -0.0383 0.0323  -0.0521 238 HIS B ND1 
4728 C CD2 . HIS B 237 ? 0.2644 0.3744 0.5976 -0.0330 0.0005  -0.0584 238 HIS B CD2 
4729 C CE1 . HIS B 237 ? 0.2570 0.3528 0.6182 -0.0380 0.0281  -0.0581 238 HIS B CE1 
4730 N NE2 . HIS B 237 ? 0.3258 0.4305 0.6837 -0.0343 0.0079  -0.0614 238 HIS B NE2 
4731 N N   . ALA B 238 ? 0.1975 0.2829 0.4622 -0.0326 0.0341  -0.0384 239 ALA B N   
4732 C CA  . ALA B 238 ? 0.2263 0.3090 0.5083 -0.0345 0.0473  -0.0393 239 ALA B CA  
4733 C C   . ALA B 238 ? 0.2089 0.3019 0.4917 -0.0311 0.0385  -0.0391 239 ALA B C   
4734 O O   . ALA B 238 ? 0.1903 0.2893 0.5025 -0.0315 0.0422  -0.0423 239 ALA B O   
4735 C CB  . ALA B 238 ? 0.2300 0.2911 0.4872 -0.0380 0.0669  -0.0345 239 ALA B CB  
4736 N N   . ASN B 239 ? 0.1950 0.2899 0.4484 -0.0277 0.0275  -0.0351 240 ASN B N   
4737 C CA  . ASN B 239 ? 0.1750 0.2797 0.4287 -0.0242 0.0184  -0.0345 240 ASN B CA  
4738 C C   . ASN B 239 ? 0.1988 0.3192 0.4756 -0.0214 0.0014  -0.0388 240 ASN B C   
4739 O O   . ASN B 239 ? 0.2177 0.3462 0.5095 -0.0193 -0.0042 -0.0396 240 ASN B O   
4740 C CB  . ASN B 239 ? 0.1820 0.2828 0.3992 -0.0217 0.0130  -0.0289 240 ASN B CB  
4741 C CG  . ASN B 239 ? 0.1854 0.2717 0.3821 -0.0238 0.0263  -0.0250 240 ASN B CG  
4742 O OD1 . ASN B 239 ? 0.2357 0.3236 0.4335 -0.0228 0.0280  -0.0245 240 ASN B OD1 
4743 N ND2 . ASN B 239 ? 0.2503 0.3208 0.4275 -0.0268 0.0354  -0.0223 240 ASN B ND2 
4744 N N   . LEU B 240 ? 0.1392 0.2624 0.4183 -0.0213 -0.0074 -0.0417 241 LEU B N   
4745 C CA  . LEU B 240 ? 0.1922 0.3231 0.4824 -0.0186 -0.0242 -0.0455 241 LEU B CA  
4746 C C   . LEU B 240 ? 0.1894 0.3171 0.5066 -0.0194 -0.0222 -0.0492 241 LEU B C   
4747 O O   . LEU B 240 ? 0.1829 0.3124 0.5058 -0.0166 -0.0349 -0.0507 241 LEU B O   
4748 C CB  . LEU B 240 ? 0.2268 0.3582 0.5050 -0.0183 -0.0336 -0.0478 241 LEU B CB  
4749 C CG  . LEU B 240 ? 0.2124 0.3442 0.4588 -0.0151 -0.0412 -0.0444 241 LEU B CG  
4750 C CD1 . LEU B 240 ? 0.2191 0.3470 0.4540 -0.0154 -0.0449 -0.0467 241 LEU B CD1 
4751 C CD2 . LEU B 240 ? 0.1872 0.3235 0.4267 -0.0110 -0.0545 -0.0438 241 LEU B CD2 
4752 N N   . ASN B 241 ? 0.2578 0.2788 0.4687 0.0078  -0.0600 -0.0560 242 ASN B N   
4753 C CA  . ASN B 241 ? 0.2582 0.2812 0.5131 0.0072  -0.0631 -0.0665 242 ASN B CA  
4754 C C   . ASN B 241 ? 0.2530 0.2793 0.5333 0.0015  -0.0430 -0.0691 242 ASN B C   
4755 O O   . ASN B 241 ? 0.2557 0.2817 0.5561 -0.0021 -0.0299 -0.0733 242 ASN B O   
4756 C CB  . ASN B 241 ? 0.3538 0.3749 0.6150 0.0076  -0.0662 -0.0706 242 ASN B CB  
4757 C CG  . ASN B 241 ? 0.3644 0.3797 0.6135 0.0141  -0.0897 -0.0722 242 ASN B CG  
4758 O OD1 . ASN B 241 ? 0.4362 0.4496 0.7094 0.0179  -0.1067 -0.0798 242 ASN B OD1 
4759 N ND2 . ASN B 241 ? 0.3711 0.3816 0.5813 0.0162  -0.0913 -0.0652 242 ASN B ND2 
4760 N N   . PRO B 242 ? 0.2495 0.2772 0.5289 0.0008  -0.0392 -0.0667 243 PRO B N   
4761 C CA  . PRO B 242 ? 0.2470 0.2749 0.5469 -0.0042 -0.0187 -0.0689 243 PRO B CA  
4762 C C   . PRO B 242 ? 0.2473 0.2778 0.5994 -0.0057 -0.0171 -0.0802 243 PRO B C   
4763 O O   . PRO B 242 ? 0.2498 0.2777 0.6212 -0.0105 0.0038  -0.0831 243 PRO B O   
4764 C CB  . PRO B 242 ? 0.2450 0.2737 0.5320 -0.0035 -0.0199 -0.0644 243 PRO B CB  
4765 C CG  . PRO B 242 ? 0.2718 0.3019 0.5558 0.0021  -0.0442 -0.0651 243 PRO B CG  
4766 C CD  . PRO B 242 ? 0.2509 0.2783 0.5135 0.0047  -0.0534 -0.0629 243 PRO B CD  
4767 N N   . GLN B 243 ? 0.2488 0.2823 0.6245 -0.0015 -0.0386 -0.0872 244 GLN B N   
4768 C CA  . GLN B 243 ? 0.2489 0.2859 0.6805 -0.0026 -0.0392 -0.0994 244 GLN B CA  
4769 C C   . GLN B 243 ? 0.2504 0.2863 0.7020 -0.0059 -0.0286 -0.1044 244 GLN B C   
4770 O O   . GLN B 243 ? 0.2506 0.2892 0.7529 -0.0080 -0.0248 -0.1151 244 GLN B O   
4771 C CB  . GLN B 243 ? 0.2529 0.2913 0.7030 0.0039  -0.0684 -0.1061 244 GLN B CB  
4772 C CG  . GLN B 243 ? 0.2598 0.2945 0.6999 0.0087  -0.0886 -0.1082 244 GLN B CG  
4773 C CD  . GLN B 243 ? 0.3098 0.3389 0.6910 0.0111  -0.0927 -0.0967 244 GLN B CD  
4774 O OE1 . GLN B 243 ? 0.2914 0.3199 0.6396 0.0101  -0.0843 -0.0873 244 GLN B OE1 
4775 N NE2 . GLN B 243 ? 0.3198 0.3442 0.6891 0.0145  -0.1055 -0.0978 244 GLN B NE2 
4776 N N   . LYS B 244 ? 0.2544 0.2863 0.6696 -0.0065 -0.0235 -0.0975 245 LYS B N   
4777 C CA  . LYS B 244 ? 0.2581 0.2873 0.6872 -0.0100 -0.0110 -0.1011 245 LYS B CA  
4778 C C   . LYS B 244 ? 0.2570 0.2794 0.6802 -0.0161 0.0200  -0.0977 245 LYS B C   
4779 O O   . LYS B 244 ? 0.3103 0.3276 0.7401 -0.0193 0.0340  -0.0996 245 LYS B O   
4780 C CB  . LYS B 244 ? 0.2565 0.2833 0.6503 -0.0069 -0.0224 -0.0961 245 LYS B CB  
4781 C CG  . LYS B 244 ? 0.2644 0.2928 0.6617 -0.0003 -0.0525 -0.1003 245 LYS B CG  
4782 C CD  . LYS B 244 ? 0.3089 0.3333 0.6797 0.0024  -0.0619 -0.0977 245 LYS B CD  
4783 C CE  . LYS B 244 ? 0.3272 0.3496 0.7149 0.0086  -0.0899 -0.1060 245 LYS B CE  
4784 N NZ  . LYS B 244 ? 0.3998 0.4162 0.7577 0.0119  -0.0996 -0.1032 245 LYS B NZ  
4785 N N   . TYR B 245 ? 0.2568 0.2770 0.6672 -0.0175 0.0311  -0.0931 246 TYR B N   
4786 C CA  . TYR B 245 ? 0.2654 0.2745 0.6621 -0.0221 0.0594  -0.0893 246 TYR B CA  
4787 C C   . TYR B 245 ? 0.2673 0.2747 0.7055 -0.0256 0.0753  -0.0965 246 TYR B C   
4788 O O   . TYR B 245 ? 0.2684 0.2851 0.7401 -0.0239 0.0622  -0.1027 246 TYR B O   
4789 C CB  . TYR B 245 ? 0.2650 0.2697 0.6089 -0.0206 0.0605  -0.0780 246 TYR B CB  
4790 C CG  . TYR B 245 ? 0.2936 0.2972 0.5977 -0.0182 0.0521  -0.0711 246 TYR B CG  
4791 C CD1 . TYR B 245 ? 0.2617 0.2741 0.5614 -0.0140 0.0283  -0.0709 246 TYR B CD1 
4792 C CD2 . TYR B 245 ? 0.3228 0.3144 0.5934 -0.0197 0.0682  -0.0652 246 TYR B CD2 
4793 C CE1 . TYR B 245 ? 0.2845 0.2954 0.5500 -0.0119 0.0222  -0.0650 246 TYR B CE1 
4794 C CE2 . TYR B 245 ? 0.3648 0.3560 0.6022 -0.0174 0.0603  -0.0595 246 TYR B CE2 
4795 C CZ  . TYR B 245 ? 0.3177 0.3194 0.5541 -0.0138 0.0382  -0.0594 246 TYR B CZ  
4796 O OH  . TYR B 245 ? 0.2971 0.2979 0.5021 -0.0115 0.0318  -0.0541 246 TYR B OH  
4797 N N   . PRO B 246 ? 0.2962 0.2896 0.7329 -0.0302 0.1045  -0.0962 247 PRO B N   
4798 C CA  . PRO B 246 ? 0.3177 0.3066 0.7894 -0.0336 0.1233  -0.1022 247 PRO B CA  
4799 C C   . PRO B 246 ? 0.2823 0.2762 0.7449 -0.0313 0.1145  -0.0992 247 PRO B C   
4800 O O   . PRO B 246 ? 0.2981 0.2937 0.7170 -0.0281 0.1018  -0.0904 247 PRO B O   
4801 C CB  . PRO B 246 ? 0.3623 0.3292 0.8089 -0.0376 0.1554  -0.0983 247 PRO B CB  
4802 C CG  . PRO B 246 ? 0.3329 0.2958 0.7561 -0.0372 0.1532  -0.0950 247 PRO B CG  
4803 C CD  . PRO B 246 ? 0.2915 0.2702 0.6952 -0.0322 0.1216  -0.0909 247 PRO B CD  
4804 N N   . ALA B 247 ? 0.2796 0.2758 0.7847 -0.0330 0.1220  -0.1067 248 ALA B N   
4805 C CA  . ALA B 247 ? 0.3219 0.3259 0.8276 -0.0302 0.1085  -0.1057 248 ALA B CA  
4806 C C   . ALA B 247 ? 0.3382 0.3316 0.7919 -0.0300 0.1179  -0.0953 248 ALA B C   
4807 O O   . ALA B 247 ? 0.3549 0.3552 0.7902 -0.0267 0.1010  -0.0908 248 ALA B O   
4808 C CB  . ALA B 247 ? 0.3235 0.3311 0.8888 -0.0322 0.1166  -0.1167 248 ALA B CB  
4809 N N   . ASP B 248 ? 0.3490 0.3237 0.7776 -0.0331 0.1442  -0.0916 249 ASP B N   
4810 C CA  . ASP B 248 ? 0.3616 0.3240 0.7442 -0.0323 0.1523  -0.0833 249 ASP B CA  
4811 C C   . ASP B 248 ? 0.3780 0.3433 0.7100 -0.0287 0.1346  -0.0736 249 ASP B C   
4812 O O   . ASP B 248 ? 0.3855 0.3520 0.6915 -0.0266 0.1263  -0.0681 249 ASP B O   
4813 C CB  . ASP B 248 ? 0.4299 0.3666 0.7958 -0.0356 0.1848  -0.0825 249 ASP B CB  
4814 C CG  . ASP B 248 ? 0.4539 0.3847 0.8667 -0.0393 0.2066  -0.0913 249 ASP B CG  
4815 O OD1 . ASP B 248 ? 0.4376 0.3835 0.8895 -0.0389 0.1964  -0.0970 249 ASP B OD1 
4816 O OD2 . ASP B 248 ? 0.4878 0.3971 0.8976 -0.0425 0.2350  -0.0927 249 ASP B OD2 
4817 N N   . ILE B 249 ? 0.3187 0.2847 0.6378 -0.0282 0.1295  -0.0718 250 ILE B N   
4818 C CA  . ILE B 249 ? 0.3615 0.3316 0.6378 -0.0248 0.1124  -0.0635 250 ILE B CA  
4819 C C   . ILE B 249 ? 0.3108 0.3006 0.6010 -0.0216 0.0850  -0.0643 250 ILE B C   
4820 O O   . ILE B 249 ? 0.2970 0.2914 0.5570 -0.0187 0.0708  -0.0577 250 ILE B O   
4821 C CB  . ILE B 249 ? 0.3615 0.3227 0.6139 -0.0250 0.1183  -0.0606 250 ILE B CB  
4822 C CG1 . ILE B 249 ? 0.3465 0.3076 0.5511 -0.0216 0.1060  -0.0517 250 ILE B CG1 
4823 C CG2 . ILE B 249 ? 0.2906 0.2627 0.5748 -0.0253 0.1092  -0.0663 250 ILE B CG2 
4824 C CD1 . ILE B 249 ? 0.3893 0.3369 0.5589 -0.0208 0.1139  -0.0463 250 ILE B CD1 
4825 N N   . GLN B 250 ? 0.2864 0.2861 0.6220 -0.0217 0.0774  -0.0727 251 GLN B N   
4826 C CA  . GLN B 250 ? 0.2807 0.2943 0.6279 -0.0178 0.0509  -0.0742 251 GLN B CA  
4827 C C   . GLN B 250 ? 0.2836 0.3000 0.6247 -0.0162 0.0446  -0.0716 251 GLN B C   
4828 O O   . GLN B 250 ? 0.2678 0.2890 0.5852 -0.0127 0.0273  -0.0663 251 GLN B O   
4829 C CB  . GLN B 250 ? 0.3025 0.3233 0.7025 -0.0177 0.0432  -0.0853 251 GLN B CB  
4830 C CG  . GLN B 250 ? 0.2459 0.2766 0.6581 -0.0124 0.0146  -0.0880 251 GLN B CG  
4831 C CD  . GLN B 250 ? 0.3515 0.3880 0.8223 -0.0120 0.0080  -0.1004 251 GLN B CD  
4832 O OE1 . GLN B 250 ? 0.3486 0.3898 0.8364 -0.0077 -0.0149 -0.1058 251 GLN B OE1 
4833 N NE2 . GLN B 250 ? 0.3812 0.4158 0.8833 -0.0160 0.0277  -0.1054 251 GLN B NE2 
4834 N N   . ARG B 251 ? 0.2858 0.2979 0.6477 -0.0188 0.0600  -0.0752 252 ARG B N   
4835 C CA  . ARG B 251 ? 0.3151 0.3290 0.6709 -0.0175 0.0556  -0.0728 252 ARG B CA  
4836 C C   . ARG B 251 ? 0.2876 0.2955 0.5922 -0.0168 0.0572  -0.0626 252 ARG B C   
4837 O O   . ARG B 251 ? 0.2965 0.3092 0.5865 -0.0144 0.0440  -0.0585 252 ARG B O   
4838 C CB  . ARG B 251 ? 0.3283 0.3370 0.7158 -0.0205 0.0743  -0.0789 252 ARG B CB  
4839 C CG  . ARG B 251 ? 0.3520 0.3699 0.7977 -0.0203 0.0675  -0.0901 252 ARG B CG  
4840 C CD  . ARG B 251 ? 0.4869 0.5008 0.9634 -0.0228 0.0846  -0.0956 252 ARG B CD  
4841 N NE  . ARG B 251 ? 0.5524 0.5622 1.0714 -0.0267 0.1042  -0.1046 252 ARG B NE  
4842 C CZ  . ARG B 251 ? 0.5602 0.5539 1.0684 -0.0309 0.1335  -0.1034 252 ARG B CZ  
4843 N NH1 . ARG B 251 ? 0.5308 0.5104 0.9864 -0.0312 0.1449  -0.0941 252 ARG B NH1 
4844 N NH2 . ARG B 251 ? 0.4713 0.4611 1.0223 -0.0346 0.1516  -0.1121 252 ARG B NH2 
4845 N N   . ALA B 252 ? 0.3065 0.3026 0.5839 -0.0187 0.0730  -0.0588 253 ALA B N   
4846 C CA  . ALA B 252 ? 0.2930 0.2830 0.5238 -0.0175 0.0724  -0.0501 253 ALA B CA  
4847 C C   . ALA B 252 ? 0.3107 0.3113 0.5233 -0.0143 0.0511  -0.0453 253 ALA B C   
4848 O O   . ALA B 252 ? 0.2738 0.2767 0.4650 -0.0126 0.0428  -0.0401 253 ALA B O   
4849 C CB  . ALA B 252 ? 0.3568 0.3304 0.5620 -0.0190 0.0901  -0.0478 253 ALA B CB  
4850 N N   . ILE B 253 ? 0.2645 0.2704 0.4849 -0.0134 0.0433  -0.0471 254 ILE B N   
4851 C CA  . ILE B 253 ? 0.2859 0.2987 0.4865 -0.0103 0.0254  -0.0425 254 ILE B CA  
4852 C C   . ILE B 253 ? 0.2933 0.3139 0.5026 -0.0075 0.0085  -0.0427 254 ILE B C   
4853 O O   . ILE B 253 ? 0.2830 0.3051 0.4676 -0.0056 -0.0004 -0.0368 254 ILE B O   
4854 C CB  . ILE B 253 ? 0.2488 0.2636 0.4574 -0.0097 0.0211  -0.0453 254 ILE B CB  
4855 C CG1 . ILE B 253 ? 0.2780 0.2834 0.4680 -0.0118 0.0367  -0.0431 254 ILE B CG1 
4856 C CG2 . ILE B 253 ? 0.2537 0.2743 0.4465 -0.0059 0.0019  -0.0419 254 ILE B CG2 
4857 C CD1 . ILE B 253 ? 0.2571 0.2627 0.4601 -0.0122 0.0368  -0.0470 254 ILE B CD1 
4858 N N   . ASN B 254 ? 0.2529 0.2771 0.4983 -0.0072 0.0039  -0.0499 255 ASN B N   
4859 C CA  . ASN B 254 ? 0.2484 0.2770 0.5015 -0.0039 -0.0130 -0.0507 255 ASN B CA  
4860 C C   . ASN B 254 ? 0.2841 0.3112 0.5208 -0.0044 -0.0094 -0.0457 255 ASN B C   
4861 O O   . ASN B 254 ? 0.2903 0.3187 0.5147 -0.0015 -0.0227 -0.0424 255 ASN B O   
4862 C CB  . ASN B 254 ? 0.2950 0.3268 0.5939 -0.0032 -0.0180 -0.0605 255 ASN B CB  
4863 C CG  . ASN B 254 ? 0.3341 0.3677 0.6493 -0.0009 -0.0306 -0.0660 255 ASN B CG  
4864 O OD1 . ASN B 254 ? 0.3551 0.3874 0.6450 0.0023  -0.0432 -0.0619 255 ASN B OD1 
4865 N ND2 . ASN B 254 ? 0.3327 0.3685 0.6910 -0.0023 -0.0270 -0.0755 255 ASN B ND2 
4866 N N   . GLU B 255 ? 0.2932 0.3155 0.5286 -0.0078 0.0086  -0.0454 256 GLU B N   
4867 C CA  . GLU B 255 ? 0.2964 0.3162 0.5164 -0.0082 0.0119  -0.0413 256 GLU B CA  
4868 C C   . GLU B 255 ? 0.3363 0.3562 0.5193 -0.0068 0.0050  -0.0332 256 GLU B C   
4869 O O   . GLU B 255 ? 0.2940 0.3155 0.4678 -0.0056 -0.0023 -0.0299 256 GLU B O   
4870 C CB  . GLU B 255 ? 0.3080 0.3184 0.5281 -0.0115 0.0331  -0.0426 256 GLU B CB  
4871 C CG  . GLU B 255 ? 0.3927 0.3997 0.6112 -0.0120 0.0377  -0.0418 256 GLU B CG  
4872 C CD  . GLU B 255 ? 0.4168 0.4296 0.6718 -0.0114 0.0324  -0.0478 256 GLU B CD  
4873 O OE1 . GLU B 255 ? 0.3917 0.4045 0.6803 -0.0128 0.0401  -0.0551 256 GLU B OE1 
4874 O OE2 . GLU B 255 ? 0.4202 0.4370 0.6718 -0.0095 0.0208  -0.0457 256 GLU B OE2 
4875 N N   . THR B 256 ? 0.2958 0.3141 0.4598 -0.0069 0.0071  -0.0303 257 THR B N   
4876 C CA  . THR B 256 ? 0.2559 0.2748 0.3892 -0.0056 0.0014  -0.0236 257 THR B CA  
4877 C C   . THR B 256 ? 0.2806 0.3043 0.4103 -0.0026 -0.0147 -0.0216 257 THR B C   
4878 O O   . THR B 256 ? 0.2811 0.3051 0.3883 -0.0017 -0.0183 -0.0161 257 THR B O   
4879 C CB  . THR B 256 ? 0.3339 0.3489 0.4495 -0.0062 0.0081  -0.0218 257 THR B CB  
4880 O OG1 . THR B 256 ? 0.2591 0.2776 0.3814 -0.0050 0.0015  -0.0235 257 THR B OG1 
4881 C CG2 . THR B 256 ? 0.3018 0.3069 0.4185 -0.0086 0.0249  -0.0243 257 THR B CG2 
4882 N N   . HIS B 257 ? 0.2507 0.2763 0.4010 -0.0006 -0.0244 -0.0260 258 HIS B N   
4883 C CA  . HIS B 257 ? 0.2604 0.2853 0.4014 0.0033  -0.0400 -0.0240 258 HIS B CA  
4884 C C   . HIS B 257 ? 0.2923 0.3155 0.4364 0.0052  -0.0483 -0.0235 258 HIS B C   
4885 O O   . HIS B 257 ? 0.2925 0.3110 0.4237 0.0089  -0.0604 -0.0213 258 HIS B O   
4886 C CB  . HIS B 257 ? 0.2463 0.2705 0.4026 0.0059  -0.0498 -0.0294 258 HIS B CB  
4887 C CG  . HIS B 257 ? 0.2646 0.2895 0.4160 0.0046  -0.0439 -0.0297 258 HIS B CG  
4888 N ND1 . HIS B 257 ? 0.2975 0.3223 0.4664 0.0060  -0.0500 -0.0355 258 HIS B ND1 
4889 C CD2 . HIS B 257 ? 0.2778 0.3028 0.4097 0.0024  -0.0333 -0.0253 258 HIS B CD2 
4890 C CE1 . HIS B 257 ? 0.2668 0.2917 0.4260 0.0044  -0.0423 -0.0342 258 HIS B CE1 
4891 N NE2 . HIS B 257 ? 0.2682 0.2929 0.4045 0.0024  -0.0323 -0.0280 258 HIS B NE2 
4892 N N   . GLN B 258 ? 0.2725 0.2973 0.4321 0.0032  -0.0419 -0.0257 259 GLN B N   
4893 C CA  . GLN B 258 ? 0.2811 0.3040 0.4455 0.0052  -0.0499 -0.0257 259 GLN B CA  
4894 C C   . GLN B 258 ? 0.3035 0.3248 0.4424 0.0043  -0.0471 -0.0186 259 GLN B C   
4895 O O   . GLN B 258 ? 0.2966 0.3195 0.4291 0.0010  -0.0355 -0.0166 259 GLN B O   
4896 C CB  . GLN B 258 ? 0.3224 0.3477 0.5170 0.0034  -0.0438 -0.0318 259 GLN B CB  
4897 C CG  . GLN B 258 ? 0.3634 0.3869 0.5608 0.0047  -0.0491 -0.0311 259 GLN B CG  
4898 C CD  . GLN B 258 ? 0.4111 0.4367 0.6404 0.0032  -0.0426 -0.0375 259 GLN B CD  
4899 O OE1 . GLN B 258 ? 0.4615 0.4890 0.7109 0.0008  -0.0320 -0.0425 259 GLN B OE1 
4900 N NE2 . GLN B 258 ? 0.4473 0.4714 0.6822 0.0047  -0.0479 -0.0377 259 GLN B NE2 
4901 N N   . GLY B 259 ? 0.3047 0.3208 0.4288 0.0074  -0.0576 -0.0150 260 GLY B N   
4902 C CA  . GLY B 259 ? 0.3502 0.3644 0.4542 0.0063  -0.0543 -0.0087 260 GLY B CA  
4903 C C   . GLY B 259 ? 0.2766 0.2921 0.3920 0.0046  -0.0504 -0.0098 260 GLY B C   
4904 O O   . GLY B 259 ? 0.2898 0.3045 0.4244 0.0062  -0.0557 -0.0142 260 GLY B O   
4905 N N   . ARG B 260 ? 0.2474 0.2648 0.3525 0.0015  -0.0414 -0.0064 261 ARG B N   
4906 C CA  . ARG B 260 ? 0.2455 0.2632 0.3591 -0.0002 -0.0367 -0.0074 261 ARG B CA  
4907 C C   . ARG B 260 ? 0.3180 0.3323 0.4204 0.0002  -0.0404 -0.0030 261 ARG B C   
4908 O O   . ARG B 260 ? 0.2590 0.2722 0.3701 -0.0003 -0.0399 -0.0042 261 ARG B O   
4909 C CB  . ARG B 260 ? 0.2800 0.2990 0.3898 -0.0035 -0.0247 -0.0078 261 ARG B CB  
4910 C CG  . ARG B 260 ? 0.2834 0.3032 0.4003 -0.0041 -0.0188 -0.0115 261 ARG B CG  
4911 C CD  . ARG B 260 ? 0.3333 0.3535 0.4774 -0.0037 -0.0180 -0.0177 261 ARG B CD  
4912 N NE  . ARG B 260 ? 0.3360 0.3562 0.4900 -0.0047 -0.0111 -0.0216 261 ARG B NE  
4913 C CZ  . ARG B 260 ? 0.3469 0.3661 0.5253 -0.0057 -0.0038 -0.0276 261 ARG B CZ  
4914 N NH1 . ARG B 260 ? 0.3016 0.3201 0.4972 -0.0059 -0.0024 -0.0305 261 ARG B NH1 
4915 N NH2 . ARG B 260 ? 0.3346 0.3529 0.5215 -0.0068 0.0033  -0.0308 261 ARG B NH2 
4916 N N   . TYR B 261 ? 0.2685 0.2800 0.3525 0.0010  -0.0429 0.0018  262 TYR B N   
4917 C CA  . TYR B 261 ? 0.2965 0.3024 0.3692 0.0015  -0.0452 0.0063  262 TYR B CA  
4918 C C   . TYR B 261 ? 0.2672 0.2688 0.3213 0.0026  -0.0458 0.0106  262 TYR B C   
4919 O O   . TYR B 261 ? 0.2647 0.2691 0.3157 0.0029  -0.0449 0.0099  262 TYR B O   
4920 C CB  . TYR B 261 ? 0.2560 0.2648 0.3292 -0.0019 -0.0383 0.0075  262 TYR B CB  
4921 C CG  . TYR B 261 ? 0.2501 0.2640 0.3173 -0.0044 -0.0314 0.0082  262 TYR B CG  
4922 C CD1 . TYR B 261 ? 0.2520 0.2657 0.3076 -0.0049 -0.0300 0.0119  262 TYR B CD1 
4923 C CD2 . TYR B 261 ? 0.2451 0.2618 0.3179 -0.0060 -0.0261 0.0047  262 TYR B CD2 
4924 C CE1 . TYR B 261 ? 0.2474 0.2655 0.2999 -0.0066 -0.0256 0.0117  262 TYR B CE1 
4925 C CE2 . TYR B 261 ? 0.2541 0.2724 0.3188 -0.0073 -0.0218 0.0050  262 TYR B CE2 
4926 C CZ  . TYR B 261 ? 0.2434 0.2634 0.2995 -0.0075 -0.0227 0.0082  262 TYR B CZ  
4927 O OH  . TYR B 261 ? 0.2422 0.2637 0.2927 -0.0081 -0.0203 0.0076  262 TYR B OH  
4928 N N   . GLN B 262 ? 0.2770 0.2706 0.3185 0.0032  -0.0461 0.0150  263 GLN B N   
4929 C CA  . GLN B 262 ? 0.3273 0.3148 0.3508 0.0040  -0.0436 0.0192  263 GLN B CA  
4930 C C   . GLN B 262 ? 0.2903 0.2774 0.3094 0.0010  -0.0355 0.0230  263 GLN B C   
4931 O O   . GLN B 262 ? 0.2864 0.2729 0.3111 -0.0005 -0.0345 0.0234  263 GLN B O   
4932 C CB  . GLN B 262 ? 0.3726 0.3437 0.3802 0.0092  -0.0518 0.0208  263 GLN B CB  
4933 C CG  . GLN B 262 ? 0.3574 0.3140 0.3531 0.0110  -0.0533 0.0242  263 GLN B CG  
4934 C CD  . GLN B 262 ? 0.4537 0.3903 0.4305 0.0175  -0.0640 0.0248  263 GLN B CD  
4935 O OE1 . GLN B 262 ? 0.4713 0.4031 0.4546 0.0210  -0.0753 0.0214  263 GLN B OE1 
4936 N NE2 . GLN B 262 ? 0.4556 0.3788 0.4086 0.0195  -0.0609 0.0287  263 GLN B NE2 
4937 N N   . VAL B 263 ? 0.2873 0.2753 0.2990 0.0000  -0.0295 0.0253  264 VAL B N   
4938 C CA  . VAL B 263 ? 0.2914 0.2773 0.3003 -0.0025 -0.0212 0.0286  264 VAL B CA  
4939 C C   . VAL B 263 ? 0.3418 0.3139 0.3314 0.0000  -0.0179 0.0326  264 VAL B C   
4940 O O   . VAL B 263 ? 0.3327 0.3071 0.3178 0.0007  -0.0164 0.0324  264 VAL B O   
4941 C CB  . VAL B 263 ? 0.2771 0.2765 0.2987 -0.0059 -0.0162 0.0266  264 VAL B CB  
4942 C CG1 . VAL B 263 ? 0.2887 0.2864 0.3124 -0.0084 -0.0078 0.0291  264 VAL B CG1 
4943 C CG2 . VAL B 263 ? 0.2831 0.2908 0.3181 -0.0077 -0.0190 0.0229  264 VAL B CG2 
4944 N N   . ASN B 264 ? 0.3796 0.3350 0.3553 0.0017  -0.0165 0.0362  265 ASN B N   
4945 C CA  . ASN B 264 ? 0.4085 0.3444 0.3596 0.0051  -0.0131 0.0402  265 ASN B CA  
4946 C C   . ASN B 264 ? 0.4282 0.3592 0.3677 0.0098  -0.0229 0.0384  265 ASN B C   
4947 O O   . ASN B 264 ? 0.4529 0.3810 0.3931 0.0130  -0.0348 0.0358  265 ASN B O   
4948 C CB  . ASN B 264 ? 0.4431 0.3809 0.3953 0.0021  0.0005  0.0423  265 ASN B CB  
4949 C CG  . ASN B 264 ? 0.5080 0.4528 0.4776 -0.0028 0.0093  0.0427  265 ASN B CG  
4950 O OD1 . ASN B 264 ? 0.5376 0.4743 0.5055 -0.0031 0.0094  0.0442  265 ASN B OD1 
4951 N ND2 . ASN B 264 ? 0.5037 0.4630 0.4911 -0.0064 0.0156  0.0408  265 ASN B ND2 
4952 N N   . THR B 265 ? 0.4056 0.3358 0.3369 0.0104  -0.0184 0.0391  266 THR B N   
4953 C CA  . THR B 265 ? 0.4106 0.3346 0.3300 0.0149  -0.0276 0.0373  266 THR B CA  
4954 C C   . THR B 265 ? 0.3530 0.2982 0.2930 0.0132  -0.0324 0.0324  266 THR B C   
4955 O O   . THR B 265 ? 0.3808 0.3233 0.3151 0.0163  -0.0395 0.0302  266 THR B O   
4956 C CB  . THR B 265 ? 0.4051 0.3133 0.3007 0.0172  -0.0201 0.0408  266 THR B CB  
4957 O OG1 . THR B 265 ? 0.4041 0.3255 0.3120 0.0125  -0.0070 0.0416  266 THR B OG1 
4958 C CG2 . THR B 265 ? 0.5016 0.3807 0.3685 0.0207  -0.0161 0.0456  266 THR B CG2 
4959 N N   . MET B 266 ? 0.3207 0.2844 0.2827 0.0085  -0.0288 0.0304  267 MET B N   
4960 C CA  . MET B 266 ? 0.3042 0.2842 0.2820 0.0069  -0.0310 0.0261  267 MET B CA  
4961 C C   . MET B 266 ? 0.3316 0.3185 0.3258 0.0062  -0.0369 0.0223  267 MET B C   
4962 O O   . MET B 266 ? 0.3385 0.3268 0.3395 0.0043  -0.0352 0.0229  267 MET B O   
4963 C CB  . MET B 266 ? 0.3340 0.3263 0.3209 0.0030  -0.0222 0.0263  267 MET B CB  
4964 C CG  . MET B 266 ? 0.3306 0.3355 0.3284 0.0019  -0.0234 0.0224  267 MET B CG  
4965 S SD  . MET B 266 ? 0.4484 0.4649 0.4581 -0.0019 -0.0171 0.0214  267 MET B SD  
4966 C CE  . MET B 266 ? 0.4104 0.4303 0.4318 -0.0035 -0.0200 0.0187  267 MET B CE  
4967 N N   . TYR B 267 ? 0.2861 0.2764 0.2877 0.0077  -0.0433 0.0183  268 TYR B N   
4968 C CA  . TYR B 267 ? 0.2922 0.2893 0.3126 0.0068  -0.0464 0.0139  268 TYR B CA  
4969 C C   . TYR B 267 ? 0.2816 0.2908 0.3129 0.0035  -0.0399 0.0115  268 TYR B C   
4970 O O   . TYR B 267 ? 0.2860 0.2978 0.3134 0.0035  -0.0380 0.0111  268 TYR B O   
4971 C CB  . TYR B 267 ? 0.3127 0.3046 0.3389 0.0106  -0.0571 0.0100  268 TYR B CB  
4972 C CG  . TYR B 267 ? 0.3425 0.3182 0.3545 0.0153  -0.0663 0.0117  268 TYR B CG  
4973 C CD1 . TYR B 267 ? 0.3675 0.3295 0.3551 0.0186  -0.0680 0.0153  268 TYR B CD1 
4974 C CD2 . TYR B 267 ? 0.3931 0.3646 0.4140 0.0170  -0.0731 0.0098  268 TYR B CD2 
4975 C CE1 . TYR B 267 ? 0.4473 0.3891 0.4161 0.0238  -0.0764 0.0171  268 TYR B CE1 
4976 C CE2 . TYR B 267 ? 0.3949 0.3481 0.3995 0.0221  -0.0828 0.0114  268 TYR B CE2 
4977 C CZ  . TYR B 267 ? 0.4561 0.3932 0.4329 0.0257  -0.0844 0.0151  268 TYR B CZ  
4978 O OH  . TYR B 267 ? 0.5295 0.4435 0.4846 0.0317  -0.0939 0.0167  268 TYR B OH  
4979 N N   . GLN B 268 ? 0.2676 0.2817 0.3100 0.0010  -0.0364 0.0098  269 GLN B N   
4980 C CA  . GLN B 268 ? 0.2629 0.2834 0.3109 -0.0014 -0.0301 0.0074  269 GLN B CA  
4981 C C   . GLN B 268 ? 0.2671 0.2884 0.3295 -0.0012 -0.0303 0.0025  269 GLN B C   
4982 O O   . GLN B 268 ? 0.2702 0.2907 0.3444 -0.0015 -0.0309 0.0002  269 GLN B O   
4983 C CB  . GLN B 268 ? 0.2445 0.2663 0.2935 -0.0038 -0.0259 0.0080  269 GLN B CB  
4984 C CG  . GLN B 268 ? 0.2553 0.2786 0.3038 -0.0052 -0.0204 0.0055  269 GLN B CG  
4985 C CD  . GLN B 268 ? 0.2486 0.2737 0.2875 -0.0049 -0.0192 0.0067  269 GLN B CD  
4986 O OE1 . GLN B 268 ? 0.2685 0.2952 0.3032 -0.0052 -0.0195 0.0090  269 GLN B OE1 
4987 N NE2 . GLN B 268 ? 0.2389 0.2636 0.2765 -0.0043 -0.0173 0.0048  269 GLN B NE2 
4988 N N   . ALA B 269 ? 0.2550 0.2777 0.3184 -0.0008 -0.0291 0.0005  270 ALA B N   
4989 C CA  . ALA B 269 ? 0.2577 0.2809 0.3367 -0.0015 -0.0258 -0.0046 270 ALA B CA  
4990 C C   . ALA B 269 ? 0.2907 0.3128 0.3645 -0.0038 -0.0154 -0.0052 270 ALA B C   
4991 O O   . ALA B 269 ? 0.2652 0.2867 0.3255 -0.0044 -0.0137 -0.0023 270 ALA B O   
4992 C CB  . ALA B 269 ? 0.2614 0.2848 0.3450 0.0004  -0.0305 -0.0068 270 ALA B CB  
4993 N N   . LEU B 270 ? 0.2611 0.2809 0.3451 -0.0047 -0.0085 -0.0093 271 LEU B N   
4994 C CA  . LEU B 270 ? 0.2920 0.3054 0.3654 -0.0060 0.0017  -0.0098 271 LEU B CA  
4995 C C   . LEU B 270 ? 0.2766 0.2899 0.3352 -0.0053 0.0014  -0.0079 271 LEU B C   
4996 O O   . LEU B 270 ? 0.3076 0.3222 0.3719 -0.0049 0.0014  -0.0095 271 LEU B O   
4997 C CB  . LEU B 270 ? 0.3247 0.3322 0.4123 -0.0074 0.0121  -0.0147 271 LEU B CB  
4998 C CG  . LEU B 270 ? 0.3580 0.3645 0.4649 -0.0083 0.0154  -0.0181 271 LEU B CG  
4999 C CD1 . LEU B 270 ? 0.3633 0.3628 0.4844 -0.0098 0.0288  -0.0232 271 LEU B CD1 
5000 C CD2 . LEU B 270 ? 0.3695 0.3714 0.4645 -0.0086 0.0171  -0.0160 271 LEU B CD2 
5001 N N   . GLY B 271 ? 0.2594 0.2712 0.3009 -0.0048 0.0004  -0.0050 272 GLY B N   
5002 C CA  . GLY B 271 ? 0.2795 0.2919 0.3087 -0.0037 -0.0010 -0.0033 272 GLY B CA  
5003 C C   . GLY B 271 ? 0.2416 0.2619 0.2715 -0.0027 -0.0085 -0.0007 272 GLY B C   
5004 O O   . GLY B 271 ? 0.2408 0.2634 0.2621 -0.0021 -0.0114 0.0020  272 GLY B O   
5005 N N   . TRP B 272 ? 0.2468 0.2695 0.2871 -0.0022 -0.0118 -0.0019 273 TRP B N   
5006 C CA  . TRP B 272 ? 0.2404 0.2659 0.2764 -0.0004 -0.0187 0.0005  273 TRP B CA  
5007 C C   . TRP B 272 ? 0.2581 0.2840 0.2914 0.0000  -0.0230 0.0037  273 TRP B C   
5008 O O   . TRP B 272 ? 0.2658 0.2911 0.3067 -0.0007 -0.0236 0.0029  273 TRP B O   
5009 C CB  . TRP B 272 ? 0.2404 0.2654 0.2872 0.0009  -0.0233 -0.0024 273 TRP B CB  
5010 C CG  . TRP B 272 ? 0.2403 0.2646 0.2910 0.0005  -0.0194 -0.0055 273 TRP B CG  
5011 C CD1 . TRP B 272 ? 0.2561 0.2788 0.3222 -0.0010 -0.0137 -0.0100 273 TRP B CD1 
5012 C CD2 . TRP B 272 ? 0.2414 0.2656 0.2817 0.0016  -0.0199 -0.0044 273 TRP B CD2 
5013 N NE1 . TRP B 272 ? 0.2416 0.2628 0.3070 -0.0011 -0.0103 -0.0117 273 TRP B NE1 
5014 C CE2 . TRP B 272 ? 0.2424 0.2649 0.2916 0.0007  -0.0148 -0.0082 273 TRP B CE2 
5015 C CE3 . TRP B 272 ? 0.2429 0.2676 0.2679 0.0033  -0.0230 -0.0007 273 TRP B CE3 
5016 C CZ2 . TRP B 272 ? 0.2524 0.2740 0.2948 0.0014  -0.0139 -0.0084 273 TRP B CZ2 
5017 C CZ3 . TRP B 272 ? 0.2441 0.2682 0.2626 0.0041  -0.0222 -0.0010 273 TRP B CZ3 
5018 C CH2 . TRP B 272 ? 0.2439 0.2667 0.2706 0.0032  -0.0182 -0.0047 273 TRP B CH2 
5019 N N   . GLU B 273 ? 0.2431 0.2686 0.2654 0.0012  -0.0251 0.0070  274 GLU B N   
5020 C CA  . GLU B 273 ? 0.2597 0.2817 0.2774 0.0022  -0.0285 0.0101  274 GLU B CA  
5021 C C   . GLU B 273 ? 0.2661 0.2818 0.2806 0.0053  -0.0356 0.0096  274 GLU B C   
5022 O O   . GLU B 273 ? 0.2585 0.2733 0.2692 0.0067  -0.0370 0.0085  274 GLU B O   
5023 C CB  . GLU B 273 ? 0.2736 0.2957 0.2815 0.0019  -0.0248 0.0138  274 GLU B CB  
5024 C CG  . GLU B 273 ? 0.2728 0.3001 0.2855 -0.0004 -0.0207 0.0134  274 GLU B CG  
5025 C CD  . GLU B 273 ? 0.4207 0.4493 0.4303 -0.0008 -0.0173 0.0158  274 GLU B CD  
5026 O OE1 . GLU B 273 ? 0.3769 0.4021 0.3788 0.0005  -0.0159 0.0182  274 GLU B OE1 
5027 O OE2 . GLU B 273 ? 0.4607 0.4929 0.4764 -0.0023 -0.0159 0.0149  274 GLU B OE2 
5028 N N   . GLU B 274 ? 0.2711 0.2809 0.2863 0.0069  -0.0411 0.0099  275 GLU B N   
5029 C CA  . GLU B 274 ? 0.2916 0.2928 0.3048 0.0108  -0.0510 0.0081  275 GLU B CA  
5030 C C   . GLU B 274 ? 0.3216 0.3092 0.3150 0.0138  -0.0543 0.0124  275 GLU B C   
5031 O O   . GLU B 274 ? 0.2992 0.2853 0.2890 0.0123  -0.0499 0.0156  275 GLU B O   
5032 C CB  . GLU B 274 ? 0.3034 0.3069 0.3371 0.0108  -0.0560 0.0032  275 GLU B CB  
5033 C CG  . GLU B 274 ? 0.3196 0.3132 0.3545 0.0156  -0.0693 0.0004  275 GLU B CG  
5034 C CD  . GLU B 274 ? 0.4078 0.4043 0.4666 0.0156  -0.0739 -0.0046 275 GLU B CD  
5035 O OE1 . GLU B 274 ? 0.5041 0.4922 0.5672 0.0200  -0.0867 -0.0080 275 GLU B OE1 
5036 O OE2 . GLU B 274 ? 0.3756 0.3812 0.4487 0.0116  -0.0652 -0.0057 275 GLU B OE2 
5037 N N   . PHE B 275 ? 0.3071 0.2826 0.2865 0.0183  -0.0618 0.0122  276 PHE B N   
5038 C CA  . PHE B 275 ? 0.3303 0.2868 0.2847 0.0222  -0.0646 0.0162  276 PHE B CA  
5039 C C   . PHE B 275 ? 0.3726 0.3138 0.3192 0.0285  -0.0799 0.0129  276 PHE B C   
5040 O O   . PHE B 275 ? 0.3464 0.2917 0.3039 0.0298  -0.0871 0.0080  276 PHE B O   
5041 C CB  . PHE B 275 ? 0.3432 0.2947 0.2783 0.0221  -0.0555 0.0206  276 PHE B CB  
5042 C CG  . PHE B 275 ? 0.3243 0.2916 0.2704 0.0166  -0.0429 0.0222  276 PHE B CG  
5043 C CD1 . PHE B 275 ? 0.3023 0.2835 0.2605 0.0144  -0.0405 0.0196  276 PHE B CD1 
5044 C CD2 . PHE B 275 ? 0.3216 0.2885 0.2664 0.0142  -0.0345 0.0258  276 PHE B CD2 
5045 C CE1 . PHE B 275 ? 0.2925 0.2857 0.2593 0.0105  -0.0314 0.0205  276 PHE B CE1 
5046 C CE2 . PHE B 275 ? 0.3341 0.3149 0.2913 0.0098  -0.0254 0.0262  276 PHE B CE2 
5047 C CZ  . PHE B 275 ? 0.3330 0.3264 0.3003 0.0084  -0.0248 0.0234  276 PHE B CZ  
5048 N N   . SER B 276 ? 0.3705 0.2921 0.2975 0.0327  -0.0854 0.0154  277 SER B N   
5049 C CA  . SER B 276 ? 0.3959 0.2961 0.3066 0.0402  -0.1015 0.0128  277 SER B CA  
5050 C C   . SER B 276 ? 0.4390 0.3277 0.3266 0.0432  -0.1010 0.0141  277 SER B C   
5051 O O   . SER B 276 ? 0.4405 0.3254 0.3103 0.0414  -0.0877 0.0196  277 SER B O   
5052 C CB  . SER B 276 ? 0.4222 0.2991 0.3094 0.0446  -0.1059 0.0163  277 SER B CB  
5053 O OG  . SER B 276 ? 0.4642 0.3166 0.3311 0.0531  -0.1231 0.0135  277 SER B OG  
5054 N N   . TYR B 277 ? 0.4607 0.3437 0.3505 0.0478  -0.1157 0.0085  278 TYR B N   
5055 C CA  . TYR B 277 ? 0.4736 0.3456 0.3426 0.0510  -0.1167 0.0088  278 TYR B CA  
5056 C C   . TYR B 277 ? 0.5111 0.3498 0.3474 0.0604  -0.1327 0.0079  278 TYR B C   
5057 O O   . TYR B 277 ? 0.5113 0.3435 0.3573 0.0650  -0.1507 0.0021  278 TYR B O   
5058 C CB  . TYR B 277 ? 0.4594 0.3501 0.3556 0.0488  -0.1205 0.0026  278 TYR B CB  
5059 C CG  . TYR B 277 ? 0.5014 0.3801 0.3763 0.0524  -0.1228 0.0024  278 TYR B CG  
5060 C CD1 . TYR B 277 ? 0.4534 0.3384 0.3184 0.0488  -0.1069 0.0072  278 TYR B CD1 
5061 C CD2 . TYR B 277 ? 0.5133 0.3734 0.3780 0.0598  -0.1418 -0.0028 278 TYR B CD2 
5062 C CE1 . TYR B 277 ? 0.5464 0.4200 0.3916 0.0521  -0.1083 0.0071  278 TYR B CE1 
5063 C CE2 . TYR B 277 ? 0.5620 0.4097 0.4055 0.0633  -0.1440 -0.0031 278 TYR B CE2 
5064 C CZ  . TYR B 277 ? 0.5502 0.4049 0.3835 0.0592  -0.1264 0.0022  278 TYR B CZ  
5065 O OH  . TYR B 277 ? 0.6058 0.4481 0.4182 0.0627  -0.1277 0.0020  278 TYR B OH  
5066 N N   . PRO B 278 ? 0.5329 0.3484 0.3305 0.0640  -0.1273 0.0127  279 PRO B N   
5067 C CA  . PRO B 278 ? 0.5669 0.3883 0.3546 0.0595  -0.1073 0.0183  279 PRO B CA  
5068 C C   . PRO B 278 ? 0.5535 0.3825 0.3433 0.0537  -0.0888 0.0246  279 PRO B C   
5069 O O   . PRO B 278 ? 0.4973 0.3119 0.2749 0.0555  -0.0893 0.0272  279 PRO B O   
5070 C CB  . PRO B 278 ? 0.6245 0.4111 0.3672 0.0671  -0.1106 0.0203  279 PRO B CB  
5071 C CG  . PRO B 278 ? 0.6766 0.4333 0.3957 0.0751  -0.1267 0.0194  279 PRO B CG  
5072 C CD  . PRO B 278 ? 0.5832 0.3605 0.3417 0.0741  -0.1424 0.0122  279 PRO B CD  
5073 N N   . ALA B 279 ? 0.4899 0.3411 0.2963 0.0470  -0.0731 0.0265  280 ALA B N   
5074 C CA  . ALA B 279 ? 0.4860 0.3458 0.2983 0.0414  -0.0559 0.0314  280 ALA B CA  
5075 C C   . ALA B 279 ? 0.5478 0.3948 0.3374 0.0415  -0.0403 0.0363  280 ALA B C   
5076 O O   . ALA B 279 ? 0.5211 0.3684 0.3052 0.0426  -0.0393 0.0352  280 ALA B O   
5077 C CB  . ALA B 279 ? 0.4463 0.3398 0.2965 0.0342  -0.0507 0.0291  280 ALA B CB  
5078 N N   . THR B 280 ? 0.4879 0.3226 0.2652 0.0404  -0.0273 0.0414  281 THR B N   
5079 C CA  . THR B 280 ? 0.5405 0.3649 0.3024 0.0395  -0.0093 0.0455  281 THR B CA  
5080 C C   . THR B 280 ? 0.5271 0.3825 0.3219 0.0326  0.0012  0.0443  281 THR B C   
5081 O O   . THR B 280 ? 0.4476 0.3289 0.2732 0.0282  -0.0027 0.0416  281 THR B O   
5082 C CB  . THR B 280 ? 0.5442 0.3457 0.2863 0.0398  0.0040  0.0509  281 THR B CB  
5083 O OG1 . THR B 280 ? 0.5094 0.3313 0.2806 0.0339  0.0080  0.0510  281 THR B OG1 
5084 C CG2 . THR B 280 ? 0.5926 0.3580 0.2961 0.0478  -0.0073 0.0522  281 THR B CG2 
5085 N N   . LEU B 281 ? 0.5278 0.3785 0.3147 0.0323  0.0144  0.0461  282 LEU B N   
5086 C CA  . LEU B 281 ? 0.4834 0.3605 0.3006 0.0266  0.0243  0.0448  282 LEU B CA  
5087 C C   . LEU B 281 ? 0.4496 0.3393 0.2902 0.0212  0.0327  0.0457  282 LEU B C   
5088 O O   . LEU B 281 ? 0.4084 0.3242 0.2793 0.0169  0.0305  0.0428  282 LEU B O   
5089 C CB  . LEU B 281 ? 0.5062 0.3732 0.3112 0.0275  0.0384  0.0465  282 LEU B CB  
5090 C CG  . LEU B 281 ? 0.4720 0.3633 0.3080 0.0225  0.0485  0.0447  282 LEU B CG  
5091 C CD1 . LEU B 281 ? 0.3951 0.3126 0.2534 0.0210  0.0353  0.0400  282 LEU B CD1 
5092 C CD2 . LEU B 281 ? 0.4815 0.3589 0.3038 0.0241  0.0635  0.0464  282 LEU B CD2 
5093 N N   . GLN B 282 ? 0.4619 0.3312 0.2870 0.0218  0.0417  0.0497  283 GLN B N   
5094 C CA  . GLN B 282 ? 0.4596 0.3396 0.3077 0.0166  0.0507  0.0504  283 GLN B CA  
5095 C C   . GLN B 282 ? 0.4438 0.3420 0.3116 0.0146  0.0369  0.0477  283 GLN B C   
5096 O O   . GLN B 282 ? 0.4152 0.3335 0.3117 0.0097  0.0396  0.0459  283 GLN B O   
5097 C CB  . GLN B 282 ? 0.5373 0.3881 0.3619 0.0178  0.0640  0.0555  283 GLN B CB  
5098 C CG  . GLN B 282 ? 0.5031 0.3634 0.3537 0.0119  0.0778  0.0561  283 GLN B CG  
5099 C CD  . GLN B 282 ? 0.5497 0.4289 0.4297 0.0077  0.0897  0.0536  283 GLN B CD  
5100 O OE1 . GLN B 282 ? 0.5157 0.4215 0.4306 0.0034  0.0861  0.0498  283 GLN B OE1 
5101 N NE2 . GLN B 282 ? 0.5516 0.4155 0.4170 0.0094  0.1032  0.0553  283 GLN B NE2 
5102 N N   . THR B 283 ? 0.4195 0.3095 0.2727 0.0186  0.0219  0.0470  284 THR B N   
5103 C CA  . THR B 283 ? 0.3999 0.3068 0.2729 0.0169  0.0094  0.0438  284 THR B CA  
5104 C C   . THR B 283 ? 0.4020 0.3365 0.3022 0.0135  0.0061  0.0395  284 THR B C   
5105 O O   . THR B 283 ? 0.3721 0.3237 0.2951 0.0097  0.0051  0.0376  284 THR B O   
5106 C CB  . THR B 283 ? 0.4464 0.3393 0.3018 0.0224  -0.0064 0.0426  284 THR B CB  
5107 O OG1 . THR B 283 ? 0.4687 0.3340 0.2977 0.0260  -0.0046 0.0465  284 THR B OG1 
5108 C CG2 . THR B 283 ? 0.3997 0.3116 0.2794 0.0207  -0.0184 0.0383  284 THR B CG2 
5109 N N   . LEU B 284 ? 0.3628 0.2994 0.2584 0.0152  0.0043  0.0380  285 LEU B N   
5110 C CA  . LEU B 284 ? 0.3531 0.3123 0.2705 0.0126  0.0014  0.0342  285 LEU B CA  
5111 C C   . LEU B 284 ? 0.3453 0.3175 0.2816 0.0085  0.0117  0.0341  285 LEU B C   
5112 O O   . LEU B 284 ? 0.3329 0.3221 0.2893 0.0058  0.0085  0.0310  285 LEU B O   
5113 C CB  . LEU B 284 ? 0.3402 0.2970 0.2474 0.0155  -0.0023 0.0328  285 LEU B CB  
5114 C CG  . LEU B 284 ? 0.4008 0.3460 0.2938 0.0200  -0.0152 0.0313  285 LEU B CG  
5115 C CD1 . LEU B 284 ? 0.3992 0.3431 0.2846 0.0225  -0.0186 0.0293  285 LEU B CD1 
5116 C CD2 . LEU B 284 ? 0.3445 0.3017 0.2561 0.0184  -0.0246 0.0278  285 LEU B CD2 
5117 N N   . LEU B 285 ? 0.3481 0.3108 0.2784 0.0083  0.0242  0.0369  286 LEU B N   
5118 C CA  . LEU B 285 ? 0.3548 0.3299 0.3080 0.0046  0.0335  0.0357  286 LEU B CA  
5119 C C   . LEU B 285 ? 0.3863 0.3682 0.3568 0.0012  0.0335  0.0351  286 LEU B C   
5120 O O   . LEU B 285 ? 0.3842 0.3820 0.3784 -0.0015 0.0326  0.0318  286 LEU B O   
5121 C CB  . LEU B 285 ? 0.3469 0.3086 0.2920 0.0050  0.0489  0.0384  286 LEU B CB  
5122 C CG  . LEU B 285 ? 0.3669 0.3233 0.2990 0.0079  0.0516  0.0384  286 LEU B CG  
5123 C CD1 . LEU B 285 ? 0.3994 0.3357 0.3175 0.0087  0.0689  0.0419  286 LEU B CD1 
5124 C CD2 . LEU B 285 ? 0.3396 0.3171 0.2950 0.0064  0.0487  0.0341  286 LEU B CD2 
5125 N N   . ASP B 286 ? 0.3676 0.3362 0.3252 0.0019  0.0334  0.0381  287 ASP B N   
5126 C CA  . ASP B 286 ? 0.3559 0.3293 0.3286 -0.0012 0.0338  0.0378  287 ASP B CA  
5127 C C   . ASP B 286 ? 0.3661 0.3566 0.3543 -0.0024 0.0219  0.0338  287 ASP B C   
5128 O O   . ASP B 286 ? 0.3373 0.3370 0.3441 -0.0054 0.0219  0.0319  287 ASP B O   
5129 C CB  . ASP B 286 ? 0.4043 0.3576 0.3567 0.0005  0.0352  0.0418  287 ASP B CB  
5130 C CG  . ASP B 286 ? 0.4882 0.4216 0.4268 0.0008  0.0511  0.0460  287 ASP B CG  
5131 O OD1 . ASP B 286 ? 0.5145 0.4537 0.4685 -0.0018 0.0627  0.0452  287 ASP B OD1 
5132 O OD2 . ASP B 286 ? 0.5604 0.4704 0.4725 0.0038  0.0525  0.0498  287 ASP B OD2 
5133 N N   . SER B 287 ? 0.3283 0.3218 0.3093 -0.0002 0.0123  0.0322  288 SER B N   
5134 C CA  . SER B 287 ? 0.3530 0.3595 0.3468 -0.0013 0.0036  0.0284  288 SER B CA  
5135 C C   . SER B 287 ? 0.3609 0.3807 0.3722 -0.0033 0.0047  0.0251  288 SER B C   
5136 O O   . SER B 287 ? 0.3484 0.3756 0.3703 -0.0046 -0.0001 0.0223  288 SER B O   
5137 C CB  . SER B 287 ? 0.3268 0.3329 0.3119 0.0013  -0.0045 0.0269  288 SER B CB  
5138 O OG  . SER B 287 ? 0.3011 0.3112 0.2845 0.0022  -0.0033 0.0258  288 SER B OG  
5139 N N   . ASN B 288 ? 0.3411 0.3623 0.3550 -0.0031 0.0106  0.0251  289 ASN B N   
5140 C CA  . ASN B 288 ? 0.3032 0.3355 0.3338 -0.0040 0.0096  0.0213  289 ASN B CA  
5141 C C   . ASN B 288 ? 0.3197 0.3545 0.3690 -0.0063 0.0168  0.0206  289 ASN B C   
5142 O O   . ASN B 288 ? 0.3100 0.3526 0.3755 -0.0064 0.0165  0.0170  289 ASN B O   
5143 C CB  . ASN B 288 ? 0.3169 0.3506 0.3413 -0.0018 0.0096  0.0205  289 ASN B CB  
5144 C CG  . ASN B 288 ? 0.3764 0.4125 0.3923 -0.0002 0.0010  0.0187  289 ASN B CG  
5145 O OD1 . ASN B 288 ? 0.3941 0.4356 0.4141 0.0006  -0.0024 0.0157  289 ASN B OD1 
5146 N ND2 . ASN B 288 ? 0.3050 0.3356 0.3099 0.0004  -0.0022 0.0202  289 ASN B ND2 
5147 N N   . SER B 289 ? 0.3313 0.3588 0.3802 -0.0080 0.0231  0.0235  290 SER B N   
5148 C CA  . SER B 289 ? 0.3408 0.3702 0.4107 -0.0108 0.0308  0.0224  290 SER B CA  
5149 C C   . SER B 289 ? 0.3229 0.3637 0.4141 -0.0121 0.0220  0.0171  290 SER B C   
5150 O O   . SER B 289 ? 0.2972 0.3405 0.3824 -0.0113 0.0119  0.0157  290 SER B O   
5151 C CB  . SER B 289 ? 0.3426 0.3592 0.4041 -0.0122 0.0389  0.0268  290 SER B CB  
5152 O OG  . SER B 289 ? 0.3670 0.3843 0.4263 -0.0127 0.0307  0.0267  290 SER B OG  
5153 N N   . GLU B 290 ? 0.2916 0.3378 0.4087 -0.0140 0.0262  0.0137  291 GLU B N   
5154 C CA  . GLU B 290 ? 0.3180 0.3725 0.4557 -0.0148 0.0166  0.0081  291 GLU B CA  
5155 C C   . GLU B 290 ? 0.3218 0.3726 0.4539 -0.0162 0.0134  0.0095  291 GLU B C   
5156 O O   . GLU B 290 ? 0.3441 0.3980 0.4774 -0.0154 0.0023  0.0061  291 GLU B O   
5157 C CB  . GLU B 290 ? 0.3508 0.4107 0.5214 -0.0168 0.0225  0.0038  291 GLU B CB  
5158 C CG  . GLU B 290 ? 0.4514 0.5181 0.6463 -0.0174 0.0116  -0.0029 291 GLU B CG  
5159 C CD  . GLU B 290 ? 0.5515 0.6233 0.7481 -0.0135 -0.0043 -0.0089 291 GLU B CD  
5160 O OE1 . GLU B 290 ? 0.6217 0.6929 0.8016 -0.0108 -0.0059 -0.0076 291 GLU B OE1 
5161 O OE2 . GLU B 290 ? 0.5882 0.6626 0.8015 -0.0128 -0.0154 -0.0151 291 GLU B OE2 
5162 N N   . GLN B 291 ? 0.3187 0.3606 0.4425 -0.0180 0.0232  0.0146  292 GLN B N   
5163 C CA  . GLN B 291 ? 0.3232 0.3610 0.4416 -0.0192 0.0202  0.0162  292 GLN B CA  
5164 C C   . GLN B 291 ? 0.3112 0.3487 0.4103 -0.0168 0.0097  0.0165  292 GLN B C   
5165 O O   . GLN B 291 ? 0.2543 0.2935 0.3560 -0.0171 0.0025  0.0143  292 GLN B O   
5166 C CB  . GLN B 291 ? 0.3031 0.3278 0.4105 -0.0204 0.0323  0.0220  292 GLN B CB  
5167 C CG  . GLN B 291 ? 0.3522 0.3714 0.4529 -0.0212 0.0291  0.0239  292 GLN B CG  
5168 C CD  . GLN B 291 ? 0.3363 0.3612 0.4621 -0.0243 0.0283  0.0201  292 GLN B CD  
5169 O OE1 . GLN B 291 ? 0.3450 0.3738 0.4940 -0.0265 0.0347  0.0174  292 GLN B OE1 
5170 N NE2 . GLN B 291 ? 0.2912 0.3162 0.4142 -0.0244 0.0205  0.0194  292 GLN B NE2 
5171 N N   . ILE B 292 ? 0.2833 0.3180 0.3642 -0.0144 0.0094  0.0188  293 ILE B N   
5172 C CA  . ILE B 292 ? 0.3047 0.3390 0.3714 -0.0124 0.0011  0.0186  293 ILE B CA  
5173 C C   . ILE B 292 ? 0.3292 0.3703 0.4007 -0.0114 -0.0069 0.0136  293 ILE B C   
5174 O O   . ILE B 292 ? 0.3026 0.3430 0.3700 -0.0109 -0.0127 0.0119  293 ILE B O   
5175 C CB  . ILE B 292 ? 0.3278 0.3561 0.3757 -0.0101 0.0025  0.0219  293 ILE B CB  
5176 C CG1 . ILE B 292 ? 0.3514 0.3676 0.3881 -0.0100 0.0079  0.0266  293 ILE B CG1 
5177 C CG2 . ILE B 292 ? 0.3390 0.3685 0.3784 -0.0084 -0.0053 0.0203  293 ILE B CG2 
5178 C CD1 . ILE B 292 ? 0.3698 0.3830 0.4072 -0.0108 0.0045  0.0270  293 ILE B CD1 
5179 N N   . PHE B 293 ? 0.2969 0.3427 0.3764 -0.0106 -0.0071 0.0112  294 PHE B N   
5180 C CA  . PHE B 293 ? 0.3128 0.3612 0.3917 -0.0085 -0.0153 0.0067  294 PHE B CA  
5181 C C   . PHE B 293 ? 0.3647 0.4138 0.4555 -0.0086 -0.0225 0.0019  294 PHE B C   
5182 O O   . PHE B 293 ? 0.3484 0.3932 0.4295 -0.0066 -0.0296 -0.0008 294 PHE B O   
5183 C CB  . PHE B 293 ? 0.3712 0.4234 0.4545 -0.0070 -0.0140 0.0055  294 PHE B CB  
5184 C CG  . PHE B 293 ? 0.4466 0.4988 0.5267 -0.0040 -0.0229 0.0010  294 PHE B CG  
5185 C CD1 . PHE B 293 ? 0.4286 0.4764 0.4896 -0.0021 -0.0250 0.0016  294 PHE B CD1 
5186 C CD2 . PHE B 293 ? 0.4905 0.5452 0.5870 -0.0028 -0.0294 -0.0044 294 PHE B CD2 
5187 C CE1 . PHE B 293 ? 0.5175 0.5614 0.5716 0.0011  -0.0323 -0.0022 294 PHE B CE1 
5188 C CE2 . PHE B 293 ? 0.5162 0.5671 0.6060 0.0009  -0.0391 -0.0088 294 PHE B CE2 
5189 C CZ  . PHE B 293 ? 0.5504 0.5948 0.6168 0.0029  -0.0399 -0.0073 294 PHE B CZ  
5190 N N   . MET B 294 ? 0.3148 0.3672 0.4260 -0.0107 -0.0204 0.0005  295 MET B N   
5191 C CA  . MET B 294 ? 0.3402 0.3933 0.4661 -0.0101 -0.0294 -0.0055 295 MET B CA  
5192 C C   . MET B 294 ? 0.3118 0.3628 0.4440 -0.0125 -0.0295 -0.0055 295 MET B C   
5193 O O   . MET B 294 ? 0.3265 0.3756 0.4662 -0.0114 -0.0388 -0.0107 295 MET B O   
5194 C CB  . MET B 294 ? 0.3973 0.4570 0.5495 -0.0103 -0.0294 -0.0096 295 MET B CB  
5195 C CG  . MET B 294 ? 0.5206 0.5820 0.6712 -0.0068 -0.0346 -0.0126 295 MET B CG  
5196 S SD  . MET B 294 ? 0.6320 0.6856 0.7691 -0.0013 -0.0521 -0.0189 295 MET B SD  
5197 C CE  . MET B 294 ? 0.4760 0.5261 0.6273 -0.0015 -0.0619 -0.0244 295 MET B CE  
5198 N N   . LYS B 295 ? 0.2855 0.3349 0.4136 -0.0151 -0.0206 -0.0001 296 LYS B N   
5199 C CA  . LYS B 295 ? 0.2625 0.3097 0.3984 -0.0176 -0.0196 0.0001  296 LYS B CA  
5200 C C   . LYS B 295 ? 0.2661 0.3077 0.3826 -0.0172 -0.0202 0.0033  296 LYS B C   
5201 O O   . LYS B 295 ? 0.2497 0.2893 0.3494 -0.0158 -0.0186 0.0063  296 LYS B O   
5202 C CB  . LYS B 295 ? 0.2477 0.2952 0.3973 -0.0209 -0.0077 0.0034  296 LYS B CB  
5203 C CG  . LYS B 295 ? 0.2881 0.3418 0.4632 -0.0217 -0.0051 -0.0006 296 LYS B CG  
5204 C CD  . LYS B 295 ? 0.4225 0.4755 0.6197 -0.0257 0.0051  -0.0002 296 LYS B CD  
5205 C CE  . LYS B 295 ? 0.4434 0.5039 0.6734 -0.0266 0.0063  -0.0062 296 LYS B CE  
5206 N NZ  . LYS B 295 ? 0.4120 0.4780 0.6536 -0.0237 -0.0113 -0.0143 296 LYS B NZ  
5207 N N   . PRO B 296 ? 0.2724 0.3111 0.3927 -0.0184 -0.0229 0.0022  297 PRO B N   
5208 C CA  . PRO B 296 ? 0.2479 0.2814 0.3535 -0.0182 -0.0221 0.0051  297 PRO B CA  
5209 C C   . PRO B 296 ? 0.2505 0.2814 0.3528 -0.0197 -0.0137 0.0110  297 PRO B C   
5210 O O   . PRO B 296 ? 0.2547 0.2851 0.3676 -0.0218 -0.0074 0.0125  297 PRO B O   
5211 C CB  . PRO B 296 ? 0.2747 0.3055 0.3875 -0.0190 -0.0271 0.0018  297 PRO B CB  
5212 C CG  . PRO B 296 ? 0.2818 0.3167 0.4172 -0.0212 -0.0262 -0.0005 297 PRO B CG  
5213 C CD  . PRO B 296 ? 0.2915 0.3315 0.4317 -0.0199 -0.0266 -0.0022 297 PRO B CD  
5214 N N   . ASN B 297 ? 0.2512 0.2781 0.3385 -0.0182 -0.0138 0.0137  298 ASN B N   
5215 C CA  . ASN B 297 ? 0.2579 0.2783 0.3368 -0.0181 -0.0087 0.0188  298 ASN B CA  
5216 C C   . ASN B 297 ? 0.2591 0.2750 0.3310 -0.0170 -0.0124 0.0194  298 ASN B C   
5217 O O   . ASN B 297 ? 0.2544 0.2723 0.3226 -0.0155 -0.0166 0.0171  298 ASN B O   
5218 C CB  . ASN B 297 ? 0.2600 0.2792 0.3279 -0.0162 -0.0061 0.0212  298 ASN B CB  
5219 C CG  . ASN B 297 ? 0.2610 0.2831 0.3367 -0.0174 -0.0004 0.0212  298 ASN B CG  
5220 O OD1 . ASN B 297 ? 0.2695 0.2861 0.3479 -0.0189 0.0076  0.0239  298 ASN B OD1 
5221 N ND2 . ASN B 297 ? 0.2848 0.3143 0.3647 -0.0166 -0.0037 0.0178  298 ASN B ND2 
5222 N N   . LYS B 298 ? 0.2666 0.2754 0.3377 -0.0177 -0.0100 0.0223  299 LYS B N   
5223 C CA  . LYS B 298 ? 0.2688 0.2728 0.3353 -0.0163 -0.0141 0.0226  299 LYS B CA  
5224 C C   . LYS B 298 ? 0.2716 0.2720 0.3265 -0.0130 -0.0173 0.0237  299 LYS B C   
5225 O O   . LYS B 298 ? 0.2911 0.2864 0.3359 -0.0116 -0.0151 0.0267  299 LYS B O   
5226 C CB  . LYS B 298 ? 0.2790 0.2740 0.3451 -0.0173 -0.0111 0.0257  299 LYS B CB  
5227 C CG  . LYS B 298 ? 0.2814 0.2716 0.3457 -0.0157 -0.0161 0.0254  299 LYS B CG  
5228 C CD  . LYS B 298 ? 0.2939 0.2731 0.3554 -0.0164 -0.0129 0.0289  299 LYS B CD  
5229 C CE  . LYS B 298 ? 0.3427 0.3159 0.4018 -0.0140 -0.0192 0.0285  299 LYS B CE  
5230 N NZ  . LYS B 298 ? 0.3792 0.3379 0.4302 -0.0135 -0.0168 0.0325  299 LYS B NZ  
5231 N N   . VAL B 299 ? 0.2669 0.2693 0.3244 -0.0116 -0.0223 0.0209  300 VAL B N   
5232 C CA  . VAL B 299 ? 0.2685 0.2688 0.3205 -0.0085 -0.0265 0.0205  300 VAL B CA  
5233 C C   . VAL B 299 ? 0.2787 0.2692 0.3273 -0.0059 -0.0314 0.0218  300 VAL B C   
5234 O O   . VAL B 299 ? 0.2817 0.2688 0.3340 -0.0066 -0.0316 0.0222  300 VAL B O   
5235 C CB  . VAL B 299 ? 0.2589 0.2662 0.3183 -0.0083 -0.0279 0.0159  300 VAL B CB  
5236 C CG1 . VAL B 299 ? 0.2524 0.2660 0.3121 -0.0102 -0.0242 0.0144  300 VAL B CG1 
5237 C CG2 . VAL B 299 ? 0.2572 0.2641 0.3263 -0.0086 -0.0291 0.0130  300 VAL B CG2 
5238 N N   . THR B 300 ? 0.2856 0.2703 0.3265 -0.0023 -0.0367 0.0220  301 THR B N   
5239 C CA  . THR B 300 ? 0.2978 0.2714 0.3347 0.0017  -0.0447 0.0221  301 THR B CA  
5240 C C   . THR B 300 ? 0.2971 0.2761 0.3471 0.0038  -0.0515 0.0168  301 THR B C   
5241 O O   . THR B 300 ? 0.2892 0.2716 0.3383 0.0047  -0.0526 0.0153  301 THR B O   
5242 C CB  . THR B 300 ? 0.3537 0.3114 0.3685 0.0051  -0.0465 0.0264  301 THR B CB  
5243 O OG1 . THR B 300 ? 0.3587 0.3110 0.3643 0.0025  -0.0371 0.0311  301 THR B OG1 
5244 C CG2 . THR B 300 ? 0.4135 0.3558 0.4206 0.0105  -0.0573 0.0261  301 THR B CG2 
5245 N N   . ALA B 301 ? 0.2889 0.2690 0.3531 0.0043  -0.0552 0.0135  302 ALA B N   
5246 C CA  . ALA B 301 ? 0.3179 0.3027 0.3998 0.0061  -0.0604 0.0076  302 ALA B CA  
5247 C C   . ALA B 301 ? 0.3388 0.3145 0.4145 0.0114  -0.0716 0.0067  302 ALA B C   
5248 O O   . ALA B 301 ? 0.3267 0.2878 0.3847 0.0150  -0.0780 0.0100  302 ALA B O   
5249 C CB  . ALA B 301 ? 0.2818 0.2673 0.3809 0.0062  -0.0621 0.0041  302 ALA B CB  
5250 N N   . ILE B 302 ? 0.3261 0.3080 0.4151 0.0122  -0.0741 0.0019  303 ILE B N   
5251 C CA  . ILE B 302 ? 0.3705 0.3439 0.4541 0.0173  -0.0858 0.0002  303 ILE B CA  
5252 C C   . ILE B 302 ? 0.4585 0.4245 0.5558 0.0222  -0.0993 -0.0046 303 ILE B C   
5253 O O   . ILE B 302 ? 0.4958 0.4700 0.6195 0.0210  -0.0983 -0.0097 303 ILE B O   
5254 C CB  . ILE B 302 ? 0.4488 0.4319 0.5439 0.0161  -0.0833 -0.0037 303 ILE B CB  
5255 C CG1 . ILE B 302 ? 0.4193 0.4149 0.5426 0.0125  -0.0758 -0.0090 303 ILE B CG1 
5256 C CG2 . ILE B 302 ? 0.3704 0.3562 0.4465 0.0134  -0.0745 0.0011  303 ILE B CG2 
5257 C CD1 . ILE B 302 ? 0.4590 0.4626 0.5919 0.0104  -0.0697 -0.0121 303 ILE B CD1 
5258 N N   . SER B 303 ? 0.4853 0.4337 0.5637 0.0284  -0.1123 -0.0033 304 SER B N   
5259 C CA  . SER B 303 ? 0.6001 0.5386 0.6899 0.0348  -0.1294 -0.0088 304 SER B CA  
5260 C C   . SER B 303 ? 0.6966 0.6327 0.7944 0.0391  -0.1417 -0.0147 304 SER B C   
5261 O O   . SER B 303 ? 0.7410 0.6872 0.8730 0.0394  -0.1464 -0.0228 304 SER B O   
5262 C CB  . SER B 303 ? 0.6241 0.5395 0.6844 0.0399  -0.1376 -0.0040 304 SER B CB  
5263 O OG  . SER B 303 ? 0.6818 0.5818 0.7065 0.0420  -0.1368 0.0019  304 SER B OG  
5264 N N   . LYS B 304 ? 0.7046 0.6273 0.7726 0.0424  -0.1458 -0.0110 305 LYS B N   
5265 C CA  . LYS B 304 ? 0.7054 0.6247 0.7767 0.0464  -0.1571 -0.0160 305 LYS B CA  
5266 C C   . LYS B 304 ? 0.6798 0.6094 0.7422 0.0414  -0.1432 -0.0124 305 LYS B C   
5267 O O   . LYS B 304 ? 0.6377 0.5582 0.6680 0.0409  -0.1362 -0.0051 305 LYS B O   
5268 C CB  . LYS B 304 ? 0.7890 0.6794 0.8293 0.0557  -0.1755 -0.0153 305 LYS B CB  
5269 C CG  . LYS B 304 ? 0.8205 0.7044 0.8690 0.0618  -0.1934 -0.0229 305 LYS B CG  
5270 C CD  . LYS B 304 ? 0.8751 0.7250 0.8843 0.0720  -0.2121 -0.0217 305 LYS B CD  
5271 C CE  . LYS B 304 ? 0.9332 0.7686 0.8969 0.0716  -0.2012 -0.0126 305 LYS B CE  
5272 N NZ  . LYS B 304 ? 0.8295 0.6796 0.8003 0.0677  -0.1934 -0.0135 305 LYS B NZ  
5273 N N   . GLU B 305 ? 0.6186 0.5660 0.7098 0.0377  -0.1384 -0.0178 306 GLU B N   
5274 C CA  . GLU B 305 ? 0.5986 0.5532 0.6813 0.0344  -0.1288 -0.0155 306 GLU B CA  
5275 C C   . GLU B 305 ? 0.5506 0.4875 0.6083 0.0408  -0.1415 -0.0151 306 GLU B C   
5276 O O   . GLU B 305 ? 0.4842 0.4088 0.5462 0.0474  -0.1598 -0.0206 306 GLU B O   
5277 C CB  . GLU B 305 ? 0.5726 0.5453 0.6900 0.0303  -0.1224 -0.0220 306 GLU B CB  
5278 C CG  . GLU B 305 ? 0.5367 0.5237 0.6536 0.0229  -0.1023 -0.0181 306 GLU B CG  
5279 C CD  . GLU B 305 ? 0.5755 0.5736 0.7142 0.0200  -0.0960 -0.0232 306 GLU B CD  
5280 O OE1 . GLU B 305 ? 0.6069 0.6067 0.7313 0.0186  -0.0905 -0.0205 306 GLU B OE1 
5281 O OE2 . GLU B 305 ? 0.6350 0.6391 0.8061 0.0192  -0.0960 -0.0302 306 GLU B OE2 
5282 N N   . PRO B 306 ? 0.5400 0.4734 0.5708 0.0395  -0.1331 -0.0091 307 PRO B N   
5283 C CA  . PRO B 306 ? 0.5942 0.5075 0.5970 0.0459  -0.1441 -0.0084 307 PRO B CA  
5284 C C   . PRO B 306 ? 0.5250 0.4407 0.5492 0.0491  -0.1577 -0.0171 307 PRO B C   
5285 O O   . PRO B 306 ? 0.4789 0.4147 0.5348 0.0443  -0.1513 -0.0216 307 PRO B O   
5286 C CB  . PRO B 306 ? 0.5127 0.4288 0.4935 0.0419  -0.1283 -0.0016 307 PRO B CB  
5287 C CG  . PRO B 306 ? 0.5162 0.4497 0.5089 0.0346  -0.1117 0.0019  307 PRO B CG  
5288 C CD  . PRO B 306 ? 0.5205 0.4683 0.5484 0.0324  -0.1139 -0.0040 307 PRO B CD  
5289 N N   . SER B 307 ? 0.5111 0.4039 0.5170 0.0576  -0.1766 -0.0198 308 SER B N   
5290 C CA  . SER B 307 ? 0.4831 0.3757 0.5112 0.0617  -0.1932 -0.0293 308 SER B CA  
5291 C C   . SER B 307 ? 0.5289 0.4302 0.5565 0.0588  -0.1858 -0.0294 308 SER B C   
5292 O O   . SER B 307 ? 0.4718 0.3878 0.5338 0.0568  -0.1878 -0.0367 308 SER B O   
5293 C CB  . SER B 307 ? 0.5809 0.4428 0.5844 0.0727  -0.2175 -0.0322 308 SER B CB  
5294 O OG  . SER B 307 ? 0.6764 0.5293 0.6831 0.0763  -0.2268 -0.0333 308 SER B OG  
5295 N N   . VAL B 308 ? 0.4954 0.3870 0.4854 0.0587  -0.1768 -0.0216 309 VAL B N   
5296 C CA  . VAL B 308 ? 0.4250 0.3221 0.4096 0.0566  -0.1701 -0.0210 309 VAL B CA  
5297 C C   . VAL B 308 ? 0.4247 0.3350 0.3998 0.0492  -0.1470 -0.0128 309 VAL B C   
5298 O O   . VAL B 308 ? 0.4406 0.3404 0.3887 0.0494  -0.1398 -0.0057 309 VAL B O   
5299 C CB  . VAL B 308 ? 0.4506 0.3199 0.3978 0.0648  -0.1833 -0.0205 309 VAL B CB  
5300 C CG1 . VAL B 308 ? 0.4970 0.3731 0.4427 0.0628  -0.1775 -0.0210 309 VAL B CG1 
5301 C CG2 . VAL B 308 ? 0.5652 0.4173 0.5186 0.0735  -0.2095 -0.0289 309 VAL B CG2 
5302 N N   . LYS B 309 ? 0.3749 0.3854 0.3713 0.0784  -0.0925 0.0228  310 LYS B N   
5303 C CA  . LYS B 309 ? 0.3513 0.3562 0.3476 0.0686  -0.0763 0.0246  310 LYS B CA  
5304 C C   . LYS B 309 ? 0.3335 0.3431 0.3268 0.0603  -0.0733 0.0187  310 LYS B C   
5305 O O   . LYS B 309 ? 0.3444 0.3638 0.3436 0.0601  -0.0818 0.0111  310 LYS B O   
5306 C CB  . LYS B 309 ? 0.3694 0.3780 0.3921 0.0642  -0.0692 0.0226  310 LYS B CB  
5307 C CG  . LYS B 309 ? 0.4293 0.4327 0.4590 0.0718  -0.0695 0.0284  310 LYS B CG  
5308 C CD  . LYS B 309 ? 0.4184 0.4300 0.4800 0.0696  -0.0671 0.0229  310 LYS B CD  
5309 C CE  . LYS B 309 ? 0.4969 0.5232 0.5783 0.0766  -0.0823 0.0170  310 LYS B CE  
5310 N NZ  . LYS B 309 ? 0.5662 0.6024 0.6811 0.0716  -0.0783 0.0087  310 LYS B NZ  
5311 N N   . MET B 310 ? 0.3183 0.3209 0.3037 0.0533  -0.0613 0.0219  311 MET B N   
5312 C CA  . MET B 310 ? 0.3151 0.3226 0.3039 0.0448  -0.0566 0.0169  311 MET B CA  
5313 C C   . MET B 310 ? 0.3142 0.3174 0.3093 0.0371  -0.0452 0.0192  311 MET B C   
5314 O O   . MET B 310 ? 0.2832 0.2784 0.2764 0.0379  -0.0401 0.0246  311 MET B O   
5315 C CB  . MET B 310 ? 0.3384 0.3414 0.3063 0.0452  -0.0560 0.0181  311 MET B CB  
5316 C CG  . MET B 310 ? 0.3498 0.3394 0.3002 0.0459  -0.0470 0.0267  311 MET B CG  
5317 S SD  . MET B 310 ? 0.4305 0.4134 0.3605 0.0447  -0.0416 0.0279  311 MET B SD  
5318 C CE  . MET B 310 ? 0.3694 0.3624 0.3187 0.0342  -0.0359 0.0229  311 MET B CE  
5319 N N   . TYR B 311 ? 0.2794 0.2871 0.2811 0.0297  -0.0416 0.0149  312 TYR B N   
5320 C CA  . TYR B 311 ? 0.3012 0.3054 0.3091 0.0222  -0.0335 0.0155  312 TYR B CA  
5321 C C   . TYR B 311 ? 0.2483 0.2534 0.2518 0.0165  -0.0301 0.0152  312 TYR B C   
5322 O O   . TYR B 311 ? 0.2562 0.2669 0.2592 0.0169  -0.0330 0.0117  312 TYR B O   
5323 C CB  . TYR B 311 ? 0.2669 0.2747 0.2916 0.0195  -0.0330 0.0099  312 TYR B CB  
5324 C CG  . TYR B 311 ? 0.2664 0.2754 0.3018 0.0254  -0.0363 0.0093  312 TYR B CG  
5325 C CD1 . TYR B 311 ? 0.3051 0.3233 0.3484 0.0313  -0.0457 0.0052  312 TYR B CD1 
5326 C CD2 . TYR B 311 ? 0.2999 0.3010 0.3387 0.0249  -0.0302 0.0125  312 TYR B CD2 
5327 C CE1 . TYR B 311 ? 0.3021 0.3229 0.3589 0.0374  -0.0501 0.0048  312 TYR B CE1 
5328 C CE2 . TYR B 311 ? 0.3127 0.3150 0.3642 0.0310  -0.0326 0.0125  312 TYR B CE2 
5329 C CZ  . TYR B 311 ? 0.3397 0.3526 0.4011 0.0376  -0.0430 0.0089  312 TYR B CZ  
5330 O OH  . TYR B 311 ? 0.3289 0.3445 0.4064 0.0442  -0.0466 0.0090  312 TYR B OH  
5331 N N   . HIS B 312 ? 0.2451 0.2447 0.2470 0.0110  -0.0241 0.0183  313 HIS B N   
5332 C CA  . HIS B 312 ? 0.2279 0.2297 0.2297 0.0058  -0.0221 0.0179  313 HIS B CA  
5333 C C   . HIS B 312 ? 0.2428 0.2398 0.2472 -0.0010 -0.0186 0.0187  313 HIS B C   
5334 O O   . HIS B 312 ? 0.2308 0.2212 0.2349 -0.0023 -0.0159 0.0198  313 HIS B O   
5335 C CB  . HIS B 312 ? 0.2812 0.2825 0.2749 0.0077  -0.0202 0.0216  313 HIS B CB  
5336 C CG  . HIS B 312 ? 0.2725 0.2670 0.2628 0.0057  -0.0144 0.0268  313 HIS B CG  
5337 N ND1 . HIS B 312 ? 0.3034 0.2951 0.2874 0.0072  -0.0100 0.0302  313 HIS B ND1 
5338 C CD2 . HIS B 312 ? 0.2564 0.2454 0.2492 0.0017  -0.0111 0.0285  313 HIS B CD2 
5339 C CE1 . HIS B 312 ? 0.2926 0.2782 0.2774 0.0043  -0.0041 0.0338  313 HIS B CE1 
5340 N NE2 . HIS B 312 ? 0.2969 0.2811 0.2869 0.0007  -0.0052 0.0326  313 HIS B NE2 
5341 N N   . LYS B 313 ? 0.2381 0.2376 0.2444 -0.0053 -0.0190 0.0178  314 LYS B N   
5342 C CA  . LYS B 313 ? 0.2595 0.2545 0.2659 -0.0117 -0.0180 0.0183  314 LYS B CA  
5343 C C   . LYS B 313 ? 0.2345 0.2347 0.2441 -0.0140 -0.0200 0.0192  314 LYS B C   
5344 O O   . LYS B 313 ? 0.2219 0.2272 0.2338 -0.0118 -0.0214 0.0177  314 LYS B O   
5345 C CB  . LYS B 313 ? 0.2386 0.2279 0.2443 -0.0142 -0.0176 0.0147  314 LYS B CB  
5346 C CG  . LYS B 313 ? 0.2614 0.2422 0.2616 -0.0209 -0.0173 0.0148  314 LYS B CG  
5347 C CD  . LYS B 313 ? 0.2750 0.2484 0.2724 -0.0232 -0.0139 0.0161  314 LYS B CD  
5348 C CE  . LYS B 313 ? 0.3225 0.2878 0.3135 -0.0307 -0.0151 0.0154  314 LYS B CE  
5349 N NZ  . LYS B 313 ? 0.3572 0.3285 0.3532 -0.0332 -0.0182 0.0177  314 LYS B NZ  
5350 N N   . THR B 314 ? 0.2551 0.2539 0.2667 -0.0185 -0.0201 0.0213  315 THR B N   
5351 C CA  . THR B 314 ? 0.2517 0.2559 0.2698 -0.0210 -0.0233 0.0221  315 THR B CA  
5352 C C   . THR B 314 ? 0.2819 0.2810 0.2965 -0.0261 -0.0282 0.0207  315 THR B C   
5353 O O   . THR B 314 ? 0.3026 0.2928 0.3097 -0.0294 -0.0275 0.0193  315 THR B O   
5354 C CB  . THR B 314 ? 0.2558 0.2634 0.2823 -0.0226 -0.0207 0.0249  315 THR B CB  
5355 O OG1 . THR B 314 ? 0.2931 0.2941 0.3174 -0.0264 -0.0185 0.0251  315 THR B OG1 
5356 C CG2 . THR B 314 ? 0.2774 0.2873 0.3037 -0.0172 -0.0150 0.0267  315 THR B CG2 
5357 N N   . GLY B 315 ? 0.2643 0.2678 0.2832 -0.0264 -0.0330 0.0214  316 GLY B N   
5358 C CA  . GLY B 315 ? 0.2676 0.2655 0.2809 -0.0305 -0.0397 0.0208  316 GLY B CA  
5359 C C   . GLY B 315 ? 0.2630 0.2697 0.2881 -0.0307 -0.0461 0.0230  316 GLY B C   
5360 O O   . GLY B 315 ? 0.2585 0.2735 0.2936 -0.0265 -0.0443 0.0247  316 GLY B O   
5361 N N   . THR B 316 ? 0.3060 0.3101 0.3300 -0.0354 -0.0541 0.0227  317 THR B N   
5362 C CA  . THR B 316 ? 0.2955 0.3093 0.3344 -0.0356 -0.0623 0.0246  317 THR B CA  
5363 C C   . THR B 316 ? 0.3235 0.3294 0.3504 -0.0386 -0.0741 0.0240  317 THR B C   
5364 O O   . THR B 316 ? 0.3125 0.3071 0.3244 -0.0436 -0.0757 0.0213  317 THR B O   
5365 C CB  . THR B 316 ? 0.3099 0.3331 0.3684 -0.0389 -0.0608 0.0244  317 THR B CB  
5366 O OG1 . THR B 316 ? 0.3160 0.3434 0.3811 -0.0355 -0.0494 0.0256  317 THR B OG1 
5367 C CG2 . THR B 316 ? 0.3614 0.3965 0.4409 -0.0392 -0.0695 0.0259  317 THR B CG2 
5368 N N   . THR B 317 ? 0.3162 0.3262 0.3478 -0.0351 -0.0821 0.0268  318 THR B N   
5369 C CA  . THR B 317 ? 0.3556 0.3593 0.3772 -0.0372 -0.0963 0.0270  318 THR B CA  
5370 C C   . THR B 317 ? 0.3359 0.3551 0.3823 -0.0349 -0.1066 0.0298  318 THR B C   
5371 O O   . THR B 317 ? 0.2867 0.3203 0.3579 -0.0322 -0.1008 0.0314  318 THR B O   
5372 C CB  . THR B 317 ? 0.3742 0.3610 0.3690 -0.0340 -0.0974 0.0284  318 THR B CB  
5373 O OG1 . THR B 317 ? 0.3552 0.3473 0.3580 -0.0268 -0.0962 0.0325  318 THR B OG1 
5374 C CG2 . THR B 317 ? 0.3497 0.3223 0.3251 -0.0356 -0.0853 0.0255  318 THR B CG2 
5375 N N   . ASN B 318 ? 0.3367 0.3516 0.3755 -0.0358 -0.1222 0.0304  319 ASN B N   
5376 C CA  . ASN B 318 ? 0.3621 0.3917 0.4254 -0.0329 -0.1347 0.0332  319 ASN B CA  
5377 C C   . ASN B 318 ? 0.3714 0.4061 0.4440 -0.0239 -0.1306 0.0387  319 ASN B C   
5378 O O   . ASN B 318 ? 0.3707 0.4194 0.4691 -0.0204 -0.1382 0.0416  319 ASN B O   
5379 C CB  . ASN B 318 ? 0.4470 0.4685 0.4950 -0.0348 -0.1543 0.0327  319 ASN B CB  
5380 C CG  . ASN B 318 ? 0.5286 0.5516 0.5800 -0.0444 -0.1616 0.0265  319 ASN B CG  
5381 O OD1 . ASN B 318 ? 0.4731 0.5098 0.5511 -0.0485 -0.1551 0.0237  319 ASN B OD1 
5382 N ND2 . ASN B 318 ? 0.5516 0.5584 0.5744 -0.0481 -0.1741 0.0241  319 ASN B ND2 
5383 N N   . ARG B 319 ? 0.3535 0.3774 0.4080 -0.0204 -0.1185 0.0397  320 ARG B N   
5384 C CA  . ARG B 319 ? 0.3318 0.3598 0.3959 -0.0127 -0.1123 0.0439  320 ARG B CA  
5385 C C   . ARG B 319 ? 0.3185 0.3414 0.3741 -0.0118 -0.0952 0.0419  320 ARG B C   
5386 O O   . ARG B 319 ? 0.3127 0.3286 0.3597 -0.0069 -0.0893 0.0437  320 ARG B O   
5387 C CB  . ARG B 319 ? 0.4237 0.4406 0.4719 -0.0070 -0.1221 0.0485  320 ARG B CB  
5388 C CG  . ARG B 319 ? 0.4517 0.4450 0.4611 -0.0088 -0.1229 0.0475  320 ARG B CG  
5389 C CD  . ARG B 319 ? 0.5038 0.4855 0.4966 -0.0039 -0.1375 0.0526  320 ARG B CD  
5390 N NE  . ARG B 319 ? 0.5620 0.5175 0.5145 -0.0058 -0.1366 0.0516  320 ARG B NE  
5391 C CZ  . ARG B 319 ? 0.5920 0.5303 0.5184 -0.0029 -0.1490 0.0552  320 ARG B CZ  
5392 N NH1 . ARG B 319 ? 0.5727 0.5187 0.5101 0.0024  -0.1657 0.0603  320 ARG B NH1 
5393 N NH2 . ARG B 319 ? 0.6370 0.5488 0.5251 -0.0053 -0.1444 0.0537  320 ARG B NH2 
5394 N N   . SER B 320 ? 0.2648 0.2915 0.3243 -0.0163 -0.0871 0.0381  321 SER B N   
5395 C CA  . SER B 320 ? 0.2677 0.2917 0.3217 -0.0148 -0.0730 0.0361  321 SER B CA  
5396 C C   . SER B 320 ? 0.2809 0.3115 0.3438 -0.0183 -0.0660 0.0334  321 SER B C   
5397 O O   . SER B 320 ? 0.2883 0.3205 0.3543 -0.0234 -0.0702 0.0321  321 SER B O   
5398 C CB  . SER B 320 ? 0.3088 0.3160 0.3361 -0.0156 -0.0697 0.0340  321 SER B CB  
5399 O OG  . SER B 320 ? 0.3363 0.3365 0.3517 -0.0215 -0.0722 0.0312  321 SER B OG  
5400 N N   . GLY B 321 ? 0.2574 0.2904 0.3229 -0.0155 -0.0552 0.0325  322 GLY B N   
5401 C CA  . GLY B 321 ? 0.2618 0.2957 0.3267 -0.0175 -0.0475 0.0302  322 GLY B CA  
5402 C C   . GLY B 321 ? 0.2606 0.2885 0.3125 -0.0148 -0.0405 0.0278  322 GLY B C   
5403 O O   . GLY B 321 ? 0.2493 0.2768 0.3009 -0.0111 -0.0382 0.0277  322 GLY B O   
5404 N N   . THR B 322 ? 0.2292 0.2522 0.2715 -0.0167 -0.0373 0.0255  323 THR B N   
5405 C CA  . THR B 322 ? 0.2251 0.2433 0.2574 -0.0146 -0.0326 0.0223  323 THR B CA  
5406 C C   . THR B 322 ? 0.2251 0.2443 0.2561 -0.0139 -0.0279 0.0214  323 THR B C   
5407 O O   . THR B 322 ? 0.2248 0.2434 0.2568 -0.0165 -0.0280 0.0227  323 THR B O   
5408 C CB  . THR B 322 ? 0.2529 0.2603 0.2722 -0.0169 -0.0344 0.0204  323 THR B CB  
5409 O OG1 . THR B 322 ? 0.3493 0.3523 0.3651 -0.0173 -0.0393 0.0222  323 THR B OG1 
5410 C CG2 . THR B 322 ? 0.2361 0.2401 0.2509 -0.0146 -0.0290 0.0165  323 THR B CG2 
5411 N N   . TYR B 323 ? 0.2096 0.2297 0.2380 -0.0103 -0.0243 0.0190  324 TYR B N   
5412 C CA  . TYR B 323 ? 0.2199 0.2391 0.2434 -0.0084 -0.0217 0.0181  324 TYR B CA  
5413 C C   . TYR B 323 ? 0.2368 0.2552 0.2564 -0.0057 -0.0216 0.0136  324 TYR B C   
5414 O O   . TYR B 323 ? 0.2309 0.2516 0.2527 -0.0041 -0.0209 0.0111  324 TYR B O   
5415 C CB  . TYR B 323 ? 0.2110 0.2331 0.2364 -0.0060 -0.0176 0.0203  324 TYR B CB  
5416 C CG  . TYR B 323 ? 0.2134 0.2317 0.2298 -0.0032 -0.0154 0.0207  324 TYR B CG  
5417 C CD1 . TYR B 323 ? 0.2387 0.2526 0.2523 -0.0048 -0.0153 0.0225  324 TYR B CD1 
5418 C CD2 . TYR B 323 ? 0.2332 0.2509 0.2424 0.0013  -0.0134 0.0194  324 TYR B CD2 
5419 C CE1 . TYR B 323 ? 0.2386 0.2476 0.2431 -0.0011 -0.0132 0.0240  324 TYR B CE1 
5420 C CE2 . TYR B 323 ? 0.2504 0.2629 0.2482 0.0050  -0.0126 0.0206  324 TYR B CE2 
5421 C CZ  . TYR B 323 ? 0.2449 0.2531 0.2409 0.0042  -0.0125 0.0233  324 TYR B CZ  
5422 O OH  . TYR B 323 ? 0.2753 0.2770 0.2593 0.0089  -0.0117 0.0254  324 TYR B OH  
5423 N N   . VAL B 324 ? 0.2275 0.2429 0.2433 -0.0051 -0.0222 0.0122  325 VAL B N   
5424 C CA  . VAL B 324 ? 0.2334 0.2500 0.2498 -0.0024 -0.0231 0.0073  325 VAL B CA  
5425 C C   . VAL B 324 ? 0.2114 0.2279 0.2238 0.0014  -0.0246 0.0080  325 VAL B C   
5426 O O   . VAL B 324 ? 0.2222 0.2346 0.2317 0.0008  -0.0236 0.0117  325 VAL B O   
5427 C CB  . VAL B 324 ? 0.2380 0.2501 0.2574 -0.0050 -0.0223 0.0041  325 VAL B CB  
5428 C CG1 . VAL B 324 ? 0.2492 0.2593 0.2695 -0.0072 -0.0207 0.0036  325 VAL B CG1 
5429 C CG2 . VAL B 324 ? 0.2471 0.2524 0.2633 -0.0078 -0.0213 0.0065  325 VAL B CG2 
5430 N N   . VAL B 325 ? 0.2340 0.2541 0.2457 0.0055  -0.0275 0.0042  326 VAL B N   
5431 C CA  . VAL B 325 ? 0.2355 0.2547 0.2408 0.0105  -0.0308 0.0052  326 VAL B CA  
5432 C C   . VAL B 325 ? 0.2595 0.2841 0.2696 0.0137  -0.0367 -0.0015 326 VAL B C   
5433 O O   . VAL B 325 ? 0.2710 0.2993 0.2845 0.0125  -0.0370 -0.0066 326 VAL B O   
5434 C CB  . VAL B 325 ? 0.2354 0.2513 0.2283 0.0130  -0.0287 0.0095  326 VAL B CB  
5435 C CG1 . VAL B 325 ? 0.2447 0.2631 0.2355 0.0131  -0.0277 0.0064  326 VAL B CG1 
5436 C CG2 . VAL B 325 ? 0.2441 0.2560 0.2258 0.0192  -0.0323 0.0114  326 VAL B CG2 
5437 N N   . PHE B 326 ? 0.2355 0.2606 0.2475 0.0177  -0.0414 -0.0018 327 PHE B N   
5438 C CA  . PHE B 326 ? 0.2739 0.3056 0.2925 0.0212  -0.0492 -0.0087 327 PHE B CA  
5439 C C   . PHE B 326 ? 0.2758 0.3067 0.2883 0.0284  -0.0568 -0.0062 327 PHE B C   
5440 O O   . PHE B 326 ? 0.2624 0.2875 0.2711 0.0303  -0.0545 0.0001  327 PHE B O   
5441 C CB  . PHE B 326 ? 0.2604 0.2971 0.2996 0.0178  -0.0479 -0.0151 327 PHE B CB  
5442 C CG  . PHE B 326 ? 0.2863 0.3207 0.3355 0.0181  -0.0459 -0.0133 327 PHE B CG  
5443 C CD1 . PHE B 326 ? 0.2443 0.2710 0.2912 0.0136  -0.0377 -0.0089 327 PHE B CD1 
5444 C CD2 . PHE B 326 ? 0.2515 0.2916 0.3142 0.0227  -0.0523 -0.0167 327 PHE B CD2 
5445 C CE1 . PHE B 326 ? 0.2334 0.2559 0.2883 0.0134  -0.0343 -0.0078 327 PHE B CE1 
5446 C CE2 . PHE B 326 ? 0.2749 0.3123 0.3490 0.0231  -0.0487 -0.0150 327 PHE B CE2 
5447 C CZ  . PHE B 326 ? 0.2645 0.2921 0.3337 0.0182  -0.0387 -0.0107 327 PHE B CZ  
5448 N N   . ILE B 327 ? 0.2535 0.2893 0.2646 0.0326  -0.0663 -0.0116 328 ILE B N   
5449 C CA  . ILE B 327 ? 0.3296 0.3642 0.3320 0.0409  -0.0764 -0.0096 328 ILE B CA  
5450 C C   . ILE B 327 ? 0.3442 0.3902 0.3656 0.0433  -0.0876 -0.0183 328 ILE B C   
5451 O O   . ILE B 327 ? 0.3461 0.3970 0.3664 0.0428  -0.0941 -0.0259 328 ILE B O   
5452 C CB  . ILE B 327 ? 0.3682 0.3943 0.3425 0.0448  -0.0787 -0.0067 328 ILE B CB  
5453 C CG1 . ILE B 327 ? 0.3542 0.3707 0.3157 0.0412  -0.0659 0.0005  328 ILE B CG1 
5454 C CG2 . ILE B 327 ? 0.3645 0.3859 0.3251 0.0543  -0.0892 -0.0030 328 ILE B CG2 
5455 C CD1 . ILE B 327 ? 0.4195 0.4280 0.3581 0.0424  -0.0637 0.0011  328 ILE B CD1 
5456 N N   . PRO B 328 ? 0.3237 0.3743 0.3647 0.0455  -0.0897 -0.0182 329 PRO B N   
5457 C CA  . PRO B 328 ? 0.3429 0.4063 0.4093 0.0469  -0.0993 -0.0276 329 PRO B CA  
5458 C C   . PRO B 328 ? 0.3675 0.4356 0.4252 0.0536  -0.1161 -0.0319 329 PRO B C   
5459 O O   . PRO B 328 ? 0.3587 0.4367 0.4303 0.0513  -0.1229 -0.0424 329 PRO B O   
5460 C CB  . PRO B 328 ? 0.3298 0.3943 0.4151 0.0499  -0.0974 -0.0241 329 PRO B CB  
5461 C CG  . PRO B 328 ? 0.3226 0.3756 0.3977 0.0450  -0.0823 -0.0163 329 PRO B CG  
5462 C CD  . PRO B 328 ? 0.3031 0.3474 0.3477 0.0454  -0.0814 -0.0107 329 PRO B CD  
5463 N N   . LYS B 329 ? 0.3418 0.4015 0.3752 0.0617  -0.1230 -0.0242 330 LYS B N   
5464 C CA  . LYS B 329 ? 0.4274 0.4889 0.4480 0.0691  -0.1408 -0.0278 330 LYS B CA  
5465 C C   . LYS B 329 ? 0.4417 0.5026 0.4479 0.0645  -0.1427 -0.0356 330 LYS B C   
5466 O O   . LYS B 329 ? 0.4424 0.5103 0.4504 0.0669  -0.1577 -0.0444 330 LYS B O   
5467 C CB  . LYS B 329 ? 0.4141 0.4613 0.4038 0.0785  -0.1447 -0.0165 330 LYS B CB  
5468 C CG  . LYS B 329 ? 0.5438 0.5877 0.5101 0.0869  -0.1632 -0.0187 330 LYS B CG  
5469 C CD  . LYS B 329 ? 0.5514 0.5744 0.4771 0.0945  -0.1610 -0.0066 330 LYS B CD  
5470 C CE  . LYS B 329 ? 0.5718 0.5865 0.4654 0.1022  -0.1776 -0.0087 330 LYS B CE  
5471 N NZ  . LYS B 329 ? 0.6528 0.6798 0.5633 0.1105  -0.1998 -0.0129 330 LYS B NZ  
5472 N N   . GLU B 330 ? 0.3824 0.4352 0.3755 0.0581  -0.1279 -0.0329 331 GLU B N   
5473 C CA  . GLU B 330 ? 0.4102 0.4599 0.3885 0.0539  -0.1267 -0.0392 331 GLU B CA  
5474 C C   . GLU B 330 ? 0.3705 0.4302 0.3746 0.0449  -0.1200 -0.0486 331 GLU B C   
5475 O O   . GLU B 330 ? 0.4176 0.4751 0.4130 0.0409  -0.1178 -0.0546 331 GLU B O   
5476 C CB  . GLU B 330 ? 0.4441 0.4778 0.3928 0.0532  -0.1141 -0.0304 331 GLU B CB  
5477 C CG  . GLU B 330 ? 0.5063 0.5264 0.4262 0.0619  -0.1178 -0.0207 331 GLU B CG  
5478 C CD  . GLU B 330 ? 0.6030 0.6178 0.4988 0.0686  -0.1334 -0.0249 331 GLU B CD  
5479 O OE1 . GLU B 330 ? 0.6302 0.6516 0.5331 0.0752  -0.1494 -0.0268 331 GLU B OE1 
5480 O OE2 . GLU B 330 ? 0.6680 0.6716 0.5375 0.0675  -0.1301 -0.0267 331 GLU B OE2 
5481 N N   . ASN B 331 ? 0.3363 0.4047 0.3706 0.0418  -0.1155 -0.0498 332 ASN B N   
5482 C CA  . ASN B 331 ? 0.3445 0.4201 0.4035 0.0338  -0.1078 -0.0582 332 ASN B CA  
5483 C C   . ASN B 331 ? 0.3408 0.4081 0.3864 0.0280  -0.0943 -0.0561 332 ASN B C   
5484 O O   . ASN B 331 ? 0.3321 0.4014 0.3833 0.0232  -0.0915 -0.0642 332 ASN B O   
5485 C CB  . ASN B 331 ? 0.3906 0.4773 0.4660 0.0331  -0.1197 -0.0718 332 ASN B CB  
5486 C CG  . ASN B 331 ? 0.3997 0.4968 0.4935 0.0392  -0.1345 -0.0744 332 ASN B CG  
5487 O OD1 . ASN B 331 ? 0.5035 0.6042 0.5893 0.0444  -0.1513 -0.0790 332 ASN B OD1 
5488 N ND2 . ASN B 331 ? 0.4862 0.5878 0.6051 0.0390  -0.1287 -0.0718 332 ASN B ND2 
5489 N N   . ILE B 332 ? 0.3489 0.4069 0.3788 0.0285  -0.0857 -0.0453 333 ILE B N   
5490 C CA  . ILE B 332 ? 0.3029 0.3536 0.3204 0.0243  -0.0744 -0.0421 333 ILE B CA  
5491 C C   . ILE B 332 ? 0.3111 0.3571 0.3301 0.0222  -0.0642 -0.0329 333 ILE B C   
5492 O O   . ILE B 332 ? 0.2999 0.3445 0.3191 0.0250  -0.0656 -0.0271 333 ILE B O   
5493 C CB  . ILE B 332 ? 0.3654 0.4074 0.3543 0.0278  -0.0767 -0.0399 333 ILE B CB  
5494 C CG1 . ILE B 332 ? 0.4045 0.4411 0.3868 0.0233  -0.0654 -0.0398 333 ILE B CG1 
5495 C CG2 . ILE B 332 ? 0.3616 0.3954 0.3327 0.0332  -0.0769 -0.0293 333 ILE B CG2 
5496 C CD1 . ILE B 332 ? 0.4244 0.4521 0.3812 0.0257  -0.0665 -0.0415 333 ILE B CD1 
5497 N N   . GLY B 333 ? 0.2585 0.3017 0.2787 0.0173  -0.0543 -0.0317 334 GLY B N   
5498 C CA  . GLY B 333 ? 0.2408 0.2793 0.2606 0.0148  -0.0462 -0.0237 334 GLY B CA  
5499 C C   . GLY B 333 ? 0.2784 0.3136 0.2938 0.0117  -0.0385 -0.0219 334 GLY B C   
5500 O O   . GLY B 333 ? 0.2588 0.2948 0.2738 0.0108  -0.0375 -0.0273 334 GLY B O   
5501 N N   . LEU B 334 ? 0.2315 0.2629 0.2451 0.0099  -0.0331 -0.0145 335 LEU B N   
5502 C CA  . LEU B 334 ? 0.2549 0.2842 0.2672 0.0077  -0.0266 -0.0116 335 LEU B CA  
5503 C C   . LEU B 334 ? 0.2399 0.2674 0.2582 0.0044  -0.0234 -0.0067 335 LEU B C   
5504 O O   . LEU B 334 ? 0.2307 0.2566 0.2483 0.0039  -0.0247 -0.0032 335 LEU B O   
5505 C CB  . LEU B 334 ? 0.2787 0.3044 0.2785 0.0102  -0.0243 -0.0073 335 LEU B CB  
5506 C CG  . LEU B 334 ? 0.2284 0.2526 0.2299 0.0087  -0.0170 -0.0042 335 LEU B CG  
5507 C CD1 . LEU B 334 ? 0.2746 0.2938 0.2630 0.0115  -0.0134 -0.0041 335 LEU B CD1 
5508 C CD2 . LEU B 334 ? 0.2511 0.2755 0.2592 0.0064  -0.0143 0.0029  335 LEU B CD2 
5509 N N   . VAL B 335 ? 0.2471 0.2738 0.2702 0.0023  -0.0194 -0.0064 336 VAL B N   
5510 C CA  . VAL B 335 ? 0.2301 0.2540 0.2561 -0.0004 -0.0179 -0.0016 336 VAL B CA  
5511 C C   . VAL B 335 ? 0.2075 0.2324 0.2357 0.0000  -0.0150 0.0024  336 VAL B C   
5512 O O   . VAL B 335 ? 0.2477 0.2730 0.2781 0.0012  -0.0117 -0.0002 336 VAL B O   
5513 C CB  . VAL B 335 ? 0.2587 0.2786 0.2889 -0.0025 -0.0161 -0.0049 336 VAL B CB  
5514 C CG1 . VAL B 335 ? 0.2379 0.2522 0.2662 -0.0046 -0.0157 0.0003  336 VAL B CG1 
5515 C CG2 . VAL B 335 ? 0.2563 0.2758 0.2890 -0.0029 -0.0175 -0.0093 336 VAL B CG2 
5516 N N   . MET B 336 ? 0.2178 0.2429 0.2474 -0.0012 -0.0160 0.0082  337 MET B N   
5517 C CA  . MET B 336 ? 0.2009 0.2281 0.2378 -0.0010 -0.0144 0.0124  337 MET B CA  
5518 C C   . MET B 336 ? 0.2007 0.2256 0.2396 -0.0033 -0.0187 0.0157  337 MET B C   
5519 O O   . MET B 336 ? 0.2013 0.2243 0.2368 -0.0059 -0.0222 0.0171  337 MET B O   
5520 C CB  . MET B 336 ? 0.2174 0.2476 0.2571 -0.0005 -0.0120 0.0159  337 MET B CB  
5521 C CG  . MET B 336 ? 0.2496 0.2837 0.3027 -0.0004 -0.0105 0.0202  337 MET B CG  
5522 S SD  . MET B 336 ? 0.3041 0.3416 0.3659 -0.0025 -0.0094 0.0246  337 MET B SD  
5523 C CE  . MET B 336 ? 0.2410 0.2780 0.3028 -0.0068 -0.0189 0.0260  337 MET B CE  
5524 N N   . LEU B 337 ? 0.2351 0.2585 0.2778 -0.0022 -0.0184 0.0169  338 LEU B N   
5525 C CA  . LEU B 337 ? 0.2189 0.2389 0.2613 -0.0033 -0.0238 0.0208  338 LEU B CA  
5526 C C   . LEU B 337 ? 0.2191 0.2450 0.2745 -0.0010 -0.0251 0.0254  338 LEU B C   
5527 O O   . LEU B 337 ? 0.2594 0.2870 0.3213 0.0021  -0.0198 0.0251  338 LEU B O   
5528 C CB  . LEU B 337 ? 0.2126 0.2225 0.2462 -0.0030 -0.0224 0.0191  338 LEU B CB  
5529 C CG  . LEU B 337 ? 0.2122 0.2166 0.2384 -0.0046 -0.0186 0.0134  338 LEU B CG  
5530 C CD1 . LEU B 337 ? 0.2483 0.2415 0.2684 -0.0044 -0.0143 0.0117  338 LEU B CD1 
5531 C CD2 . LEU B 337 ? 0.2436 0.2458 0.2635 -0.0079 -0.0218 0.0133  338 LEU B CD2 
5532 N N   . THR B 338 ? 0.2462 0.2754 0.3072 -0.0027 -0.0320 0.0292  339 THR B N   
5533 C CA  . THR B 338 ? 0.2481 0.2842 0.3257 -0.0004 -0.0350 0.0336  339 THR B CA  
5534 C C   . THR B 338 ? 0.2821 0.3147 0.3561 -0.0011 -0.0463 0.0368  339 THR B C   
5535 O O   . THR B 338 ? 0.2843 0.3094 0.3431 -0.0046 -0.0507 0.0355  339 THR B O   
5536 C CB  . THR B 338 ? 0.2491 0.2952 0.3431 -0.0017 -0.0328 0.0345  339 THR B CB  
5537 O OG1 . THR B 338 ? 0.3251 0.3715 0.4164 -0.0064 -0.0385 0.0342  339 THR B OG1 
5538 C CG2 . THR B 338 ? 0.2636 0.3097 0.3552 -0.0007 -0.0218 0.0314  339 THR B CG2 
5539 N N   . ASN B 339 ? 0.2677 0.3051 0.3553 0.0025  -0.0511 0.0412  340 ASN B N   
5540 C CA  . ASN B 339 ? 0.2471 0.2821 0.3323 0.0026  -0.0644 0.0448  340 ASN B CA  
5541 C C   . ASN B 339 ? 0.2469 0.2954 0.3547 0.0006  -0.0723 0.0463  340 ASN B C   
5542 O O   . ASN B 339 ? 0.2590 0.3103 0.3741 0.0023  -0.0846 0.0498  340 ASN B O   
5543 C CB  . ASN B 339 ? 0.2565 0.2853 0.3395 0.0090  -0.0664 0.0492  340 ASN B CB  
5544 C CG  . ASN B 339 ? 0.2411 0.2797 0.3480 0.0142  -0.0598 0.0516  340 ASN B CG  
5545 O OD1 . ASN B 339 ? 0.2439 0.2945 0.3710 0.0131  -0.0553 0.0506  340 ASN B OD1 
5546 N ND2 . ASN B 339 ? 0.2507 0.2820 0.3543 0.0200  -0.0579 0.0550  340 ASN B ND2 
5547 N N   . LYS B 340 ? 0.2354 0.2916 0.3544 -0.0029 -0.0655 0.0435  341 LYS B N   
5548 C CA  . LYS B 340 ? 0.2543 0.3220 0.3951 -0.0064 -0.0704 0.0436  341 LYS B CA  
5549 C C   . LYS B 340 ? 0.2335 0.3004 0.3705 -0.0114 -0.0616 0.0398  341 LYS B C   
5550 O O   . LYS B 340 ? 0.2394 0.3034 0.3702 -0.0099 -0.0496 0.0385  341 LYS B O   
5551 C CB  . LYS B 340 ? 0.2448 0.3255 0.4173 -0.0025 -0.0673 0.0464  341 LYS B CB  
5552 C CG  . LYS B 340 ? 0.2663 0.3600 0.4665 -0.0064 -0.0742 0.0461  341 LYS B CG  
5553 C CD  . LYS B 340 ? 0.2665 0.3704 0.4962 -0.0052 -0.0616 0.0464  341 LYS B CD  
5554 C CE  . LYS B 340 ? 0.2591 0.3776 0.5235 -0.0083 -0.0693 0.0463  341 LYS B CE  
5555 N NZ  . LYS B 340 ? 0.2317 0.3563 0.5202 -0.0098 -0.0529 0.0451  341 LYS B NZ  
5556 N N   . ARG B 341 ? 0.2416 0.3103 0.3814 -0.0172 -0.0680 0.0381  342 ARG B N   
5557 C CA  . ARG B 341 ? 0.2459 0.3131 0.3838 -0.0215 -0.0593 0.0354  342 ARG B CA  
5558 C C   . ARG B 341 ? 0.2852 0.3600 0.4438 -0.0199 -0.0469 0.0362  342 ARG B C   
5559 O O   . ARG B 341 ? 0.2718 0.3572 0.4570 -0.0188 -0.0479 0.0378  342 ARG B O   
5560 C CB  . ARG B 341 ? 0.2942 0.3620 0.4352 -0.0284 -0.0683 0.0331  342 ARG B CB  
5561 C CG  . ARG B 341 ? 0.4316 0.5034 0.5871 -0.0330 -0.0600 0.0313  342 ARG B CG  
5562 C CD  . ARG B 341 ? 0.4786 0.5575 0.6525 -0.0393 -0.0708 0.0290  342 ARG B CD  
5563 N NE  . ARG B 341 ? 0.5454 0.6139 0.6977 -0.0448 -0.0787 0.0258  342 ARG B NE  
5564 C CZ  . ARG B 341 ? 0.6103 0.6741 0.7606 -0.0511 -0.0741 0.0225  342 ARG B CZ  
5565 N NH1 . ARG B 341 ? 0.6176 0.6854 0.7851 -0.0527 -0.0617 0.0223  342 ARG B NH1 
5566 N NH2 . ARG B 341 ? 0.5559 0.6085 0.6850 -0.0559 -0.0806 0.0195  342 ARG B NH2 
5567 N N   . ILE B 342 ? 0.2458 0.3141 0.3918 -0.0195 -0.0349 0.0351  343 ILE B N   
5568 C CA  . ILE B 342 ? 0.2544 0.3247 0.4130 -0.0190 -0.0216 0.0355  343 ILE B CA  
5569 C C   . ILE B 342 ? 0.2557 0.3185 0.4022 -0.0226 -0.0160 0.0341  343 ILE B C   
5570 O O   . ILE B 342 ? 0.2730 0.3287 0.3993 -0.0240 -0.0206 0.0327  343 ILE B O   
5571 C CB  . ILE B 342 ? 0.2310 0.2978 0.3823 -0.0132 -0.0114 0.0361  343 ILE B CB  
5572 C CG1 . ILE B 342 ? 0.2658 0.3221 0.3877 -0.0117 -0.0095 0.0342  343 ILE B CG1 
5573 C CG2 . ILE B 342 ? 0.2556 0.3279 0.4171 -0.0092 -0.0162 0.0377  343 ILE B CG2 
5574 C CD1 . ILE B 342 ? 0.2980 0.3505 0.4112 -0.0067 -0.0015 0.0334  343 ILE B CD1 
5575 N N   . PRO B 343 ? 0.3026 0.3654 0.4611 -0.0240 -0.0047 0.0346  344 PRO B N   
5576 C CA  . PRO B 343 ? 0.2419 0.2956 0.3886 -0.0269 0.0017  0.0341  344 PRO B CA  
5577 C C   . PRO B 343 ? 0.2674 0.3101 0.3835 -0.0231 0.0033  0.0341  344 PRO B C   
5578 O O   . PRO B 343 ? 0.2375 0.2778 0.3429 -0.0179 0.0067  0.0344  344 PRO B O   
5579 C CB  . PRO B 343 ? 0.2786 0.3310 0.4400 -0.0267 0.0171  0.0354  344 PRO B CB  
5580 C CG  . PRO B 343 ? 0.2711 0.3368 0.4639 -0.0274 0.0147  0.0355  344 PRO B CG  
5581 C CD  . PRO B 343 ? 0.2651 0.3346 0.4497 -0.0229 0.0043  0.0359  344 PRO B CD  
5582 N N   . ASN B 344 ? 0.2633 0.2995 0.3667 -0.0259 0.0005  0.0332  345 ASN B N   
5583 C CA  . ASN B 344 ? 0.2837 0.3109 0.3623 -0.0221 0.0008  0.0330  345 ASN B CA  
5584 C C   . ASN B 344 ? 0.2963 0.3160 0.3632 -0.0169 0.0117  0.0349  345 ASN B C   
5585 O O   . ASN B 344 ? 0.2835 0.2995 0.3338 -0.0121 0.0105  0.0343  345 ASN B O   
5586 C CB  . ASN B 344 ? 0.3387 0.3594 0.4091 -0.0259 -0.0018 0.0321  345 ASN B CB  
5587 C CG  . ASN B 344 ? 0.3149 0.3383 0.3858 -0.0300 -0.0133 0.0296  345 ASN B CG  
5588 O OD1 . ASN B 344 ? 0.3557 0.3848 0.4302 -0.0289 -0.0199 0.0291  345 ASN B OD1 
5589 N ND2 . ASN B 344 ? 0.3562 0.3731 0.4214 -0.0345 -0.0150 0.0281  345 ASN B ND2 
5590 N N   . GLU B 345 ? 0.2837 0.3000 0.3585 -0.0180 0.0225  0.0369  346 GLU B N   
5591 C CA  . GLU B 345 ? 0.2528 0.2582 0.3125 -0.0128 0.0340  0.0392  346 GLU B CA  
5592 C C   . GLU B 345 ? 0.3024 0.3098 0.3587 -0.0084 0.0355  0.0384  346 GLU B C   
5593 O O   . GLU B 345 ? 0.3323 0.3307 0.3670 -0.0032 0.0387  0.0387  346 GLU B O   
5594 C CB  . GLU B 345 ? 0.2814 0.2812 0.3525 -0.0156 0.0476  0.0414  346 GLU B CB  
5595 C CG  . GLU B 345 ? 0.3736 0.3860 0.4780 -0.0209 0.0485  0.0401  346 GLU B CG  
5596 C CD  . GLU B 345 ? 0.4582 0.4777 0.5815 -0.0285 0.0416  0.0381  346 GLU B CD  
5597 O OE1 . GLU B 345 ? 0.3649 0.3858 0.4794 -0.0303 0.0297  0.0364  346 GLU B OE1 
5598 O OE2 . GLU B 345 ? 0.4953 0.5183 0.6432 -0.0331 0.0488  0.0375  346 GLU B OE2 
5599 N N   . GLU B 346 ? 0.2589 0.2775 0.3360 -0.0102 0.0328  0.0373  347 GLU B N   
5600 C CA  . GLU B 346 ? 0.2884 0.3080 0.3628 -0.0062 0.0351  0.0362  347 GLU B CA  
5601 C C   . GLU B 346 ? 0.2878 0.3072 0.3444 -0.0032 0.0256  0.0336  347 GLU B C   
5602 O O   . GLU B 346 ? 0.3091 0.3231 0.3512 0.0008  0.0288  0.0320  347 GLU B O   
5603 C CB  . GLU B 346 ? 0.2840 0.3157 0.3867 -0.0080 0.0340  0.0363  347 GLU B CB  
5604 C CG  . GLU B 346 ? 0.2873 0.3214 0.4142 -0.0110 0.0441  0.0380  347 GLU B CG  
5605 C CD  . GLU B 346 ? 0.3904 0.4174 0.5184 -0.0079 0.0602  0.0388  347 GLU B CD  
5606 O OE1 . GLU B 346 ? 0.3980 0.4131 0.4990 -0.0037 0.0652  0.0383  347 GLU B OE1 
5607 O OE2 . GLU B 346 ? 0.3634 0.3964 0.5200 -0.0098 0.0678  0.0396  347 GLU B OE2 
5608 N N   . ARG B 347 ? 0.2453 0.2696 0.3029 -0.0055 0.0145  0.0324  348 ARG B N   
5609 C CA  . ARG B 347 ? 0.2516 0.2753 0.2954 -0.0033 0.0071  0.0294  348 ARG B CA  
5610 C C   . ARG B 347 ? 0.2535 0.2684 0.2762 0.0004  0.0086  0.0288  348 ARG B C   
5611 O O   . ARG B 347 ? 0.2652 0.2783 0.2767 0.0039  0.0069  0.0258  348 ARG B O   
5612 C CB  . ARG B 347 ? 0.2322 0.2594 0.2797 -0.0068 -0.0026 0.0286  348 ARG B CB  
5613 C CG  . ARG B 347 ? 0.2837 0.3183 0.3499 -0.0105 -0.0066 0.0299  348 ARG B CG  
5614 C CD  . ARG B 347 ? 0.2576 0.2913 0.3207 -0.0142 -0.0155 0.0290  348 ARG B CD  
5615 N NE  . ARG B 347 ? 0.2645 0.3037 0.3431 -0.0183 -0.0208 0.0301  348 ARG B NE  
5616 C CZ  . ARG B 347 ? 0.2652 0.3025 0.3405 -0.0221 -0.0292 0.0292  348 ARG B CZ  
5617 N NH1 . ARG B 347 ? 0.2299 0.2594 0.2883 -0.0223 -0.0314 0.0273  348 ARG B NH1 
5618 N NH2 . ARG B 347 ? 0.2585 0.3013 0.3481 -0.0259 -0.0356 0.0298  348 ARG B NH2 
5619 N N   . ILE B 348 ? 0.2551 0.2640 0.2724 -0.0002 0.0110  0.0314  349 ILE B N   
5620 C CA  . ILE B 348 ? 0.2732 0.2728 0.2701 0.0044  0.0112  0.0319  349 ILE B CA  
5621 C C   . ILE B 348 ? 0.2711 0.2625 0.2532 0.0090  0.0183  0.0323  349 ILE B C   
5622 O O   . ILE B 348 ? 0.3093 0.2963 0.2741 0.0137  0.0142  0.0303  349 ILE B O   
5623 C CB  . ILE B 348 ? 0.2595 0.2528 0.2550 0.0029  0.0143  0.0355  349 ILE B CB  
5624 C CG1 . ILE B 348 ? 0.2640 0.2629 0.2695 -0.0018 0.0071  0.0341  349 ILE B CG1 
5625 C CG2 . ILE B 348 ? 0.2912 0.2726 0.2644 0.0091  0.0158  0.0378  349 ILE B CG2 
5626 C CD1 . ILE B 348 ? 0.2704 0.2638 0.2794 -0.0054 0.0113  0.0367  349 ILE B CD1 
5627 N N   . LYS B 349 ? 0.2883 0.2767 0.2772 0.0077  0.0292  0.0346  350 LYS B N   
5628 C CA  . LYS B 349 ? 0.3089 0.2856 0.2808 0.0118  0.0385  0.0351  350 LYS B CA  
5629 C C   . LYS B 349 ? 0.3074 0.2873 0.2747 0.0137  0.0349  0.0303  350 LYS B C   
5630 O O   . LYS B 349 ? 0.3622 0.3323 0.3063 0.0181  0.0351  0.0284  350 LYS B O   
5631 C CB  . LYS B 349 ? 0.3531 0.3263 0.3382 0.0093  0.0531  0.0381  350 LYS B CB  
5632 C CG  . LYS B 349 ? 0.3756 0.3397 0.3597 0.0081  0.0616  0.0425  350 LYS B CG  
5633 C CD  . LYS B 349 ? 0.3927 0.3566 0.3982 0.0045  0.0760  0.0441  350 LYS B CD  
5634 C CE  . LYS B 349 ? 0.5318 0.4867 0.5400 0.0021  0.0860  0.0478  350 LYS B CE  
5635 N NZ  . LYS B 349 ? 0.6076 0.5649 0.6437 -0.0024 0.0997  0.0483  350 LYS B NZ  
5636 N N   . ALA B 350 ? 0.2904 0.2827 0.2784 0.0105  0.0315  0.0281  351 ALA B N   
5637 C CA  . ALA B 350 ? 0.2855 0.2799 0.2715 0.0119  0.0301  0.0234  351 ALA B CA  
5638 C C   . ALA B 350 ? 0.3057 0.3008 0.2776 0.0140  0.0191  0.0187  351 ALA B C   
5639 O O   . ALA B 350 ? 0.3068 0.2962 0.2632 0.0167  0.0189  0.0145  351 ALA B O   
5640 C CB  . ALA B 350 ? 0.3019 0.3083 0.3134 0.0087  0.0288  0.0232  351 ALA B CB  
5641 N N   . ALA B 351 ? 0.2883 0.2898 0.2662 0.0126  0.0101  0.0189  352 ALA B N   
5642 C CA  . ALA B 351 ? 0.2815 0.2847 0.2511 0.0145  0.0002  0.0143  352 ALA B CA  
5643 C C   . ALA B 351 ? 0.3176 0.3110 0.2642 0.0196  -0.0016 0.0143  352 ALA B C   
5644 O O   . ALA B 351 ? 0.3516 0.3445 0.2881 0.0222  -0.0082 0.0089  352 ALA B O   
5645 C CB  . ALA B 351 ? 0.2914 0.3007 0.2721 0.0120  -0.0063 0.0152  352 ALA B CB  
5646 N N   . TYR B 352 ? 0.3426 0.3274 0.2805 0.0212  0.0036  0.0202  353 TYR B N   
5647 C CA  . TYR B 352 ? 0.3540 0.3262 0.2664 0.0270  0.0025  0.0218  353 TYR B CA  
5648 C C   . TYR B 352 ? 0.3972 0.3602 0.2903 0.0297  0.0059  0.0184  353 TYR B C   
5649 O O   . TYR B 352 ? 0.4269 0.3846 0.3003 0.0343  -0.0022 0.0151  353 TYR B O   
5650 C CB  . TYR B 352 ? 0.3685 0.3307 0.2760 0.0276  0.0117  0.0293  353 TYR B CB  
5651 C CG  . TYR B 352 ? 0.4267 0.3735 0.3066 0.0345  0.0108  0.0329  353 TYR B CG  
5652 C CD1 . TYR B 352 ? 0.4103 0.3581 0.2882 0.0378  0.0017  0.0347  353 TYR B CD1 
5653 C CD2 . TYR B 352 ? 0.4149 0.3444 0.2699 0.0382  0.0198  0.0351  353 TYR B CD2 
5654 C CE1 . TYR B 352 ? 0.5003 0.4335 0.3529 0.0452  0.0001  0.0389  353 TYR B CE1 
5655 C CE2 . TYR B 352 ? 0.4773 0.3900 0.3031 0.0454  0.0186  0.0392  353 TYR B CE2 
5656 C CZ  . TYR B 352 ? 0.5157 0.4310 0.3408 0.0492  0.0079  0.0414  353 TYR B CZ  
5657 O OH  . TYR B 352 ? 0.6439 0.5421 0.4400 0.0575  0.0057  0.0463  353 TYR B OH  
5658 N N   . ALA B 353 ? 0.3831 0.3435 0.2815 0.0270  0.0178  0.0189  354 ALA B N   
5659 C CA  . ALA B 353 ? 0.4272 0.3765 0.3064 0.0290  0.0233  0.0154  354 ALA B CA  
5660 C C   . ALA B 353 ? 0.4062 0.3630 0.2858 0.0287  0.0131  0.0067  354 ALA B C   
5661 O O   . ALA B 353 ? 0.4272 0.3746 0.2829 0.0319  0.0092  0.0021  354 ALA B O   
5662 C CB  . ALA B 353 ? 0.4123 0.3589 0.3037 0.0259  0.0393  0.0175  354 ALA B CB  
5663 N N   . VAL B 354 ? 0.3813 0.3537 0.2868 0.0247  0.0087  0.0040  355 VAL B N   
5664 C CA  . VAL B 354 ? 0.4025 0.3814 0.3111 0.0237  0.0010  -0.0046 355 VAL B CA  
5665 C C   . VAL B 354 ? 0.4199 0.4002 0.3177 0.0269  -0.0134 -0.0086 355 VAL B C   
5666 O O   . VAL B 354 ? 0.3922 0.3678 0.2739 0.0288  -0.0191 -0.0152 355 VAL B O   
5667 C CB  . VAL B 354 ? 0.3543 0.3467 0.2912 0.0192  0.0008  -0.0055 355 VAL B CB  
5668 C CG1 . VAL B 354 ? 0.3629 0.3615 0.3048 0.0180  -0.0069 -0.0144 355 VAL B CG1 
5669 C CG2 . VAL B 354 ? 0.3366 0.3278 0.2842 0.0172  0.0132  -0.0027 355 VAL B CG2 
5670 N N   . LEU B 355 ? 0.3864 0.3728 0.2931 0.0276  -0.0196 -0.0048 356 LEU B N   
5671 C CA  . LEU B 355 ? 0.3967 0.3873 0.3005 0.0308  -0.0335 -0.0088 356 LEU B CA  
5672 C C   . LEU B 355 ? 0.4646 0.4424 0.3381 0.0372  -0.0389 -0.0085 356 LEU B C   
5673 O O   . LEU B 355 ? 0.4699 0.4502 0.3374 0.0399  -0.0514 -0.0152 356 LEU B O   
5674 C CB  . LEU B 355 ? 0.4127 0.4104 0.3321 0.0305  -0.0368 -0.0042 356 LEU B CB  
5675 C CG  . LEU B 355 ? 0.3493 0.3581 0.2949 0.0247  -0.0345 -0.0060 356 LEU B CG  
5676 C CD1 . LEU B 355 ? 0.3810 0.3932 0.3377 0.0241  -0.0362 -0.0016 356 LEU B CD1 
5677 C CD2 . LEU B 355 ? 0.3908 0.4075 0.3467 0.0230  -0.0405 -0.0156 356 LEU B CD2 
5678 N N   . ASN B 356 ? 0.4268 0.3901 0.2809 0.0398  -0.0296 -0.0013 357 ASN B N   
5679 C CA  . ASN B 356 ? 0.5087 0.4559 0.3288 0.0466  -0.0339 0.0000  357 ASN B CA  
5680 C C   . ASN B 356 ? 0.5405 0.4777 0.3390 0.0467  -0.0330 -0.0071 357 ASN B C   
5681 O O   . ASN B 356 ? 0.5540 0.4798 0.3235 0.0522  -0.0420 -0.0091 357 ASN B O   
5682 C CB  . ASN B 356 ? 0.4731 0.4050 0.2784 0.0493  -0.0221 0.0103  357 ASN B CB  
5683 C CG  . ASN B 356 ? 0.5625 0.4981 0.3756 0.0522  -0.0275 0.0164  357 ASN B CG  
5684 O OD1 . ASN B 356 ? 0.6367 0.5656 0.4317 0.0593  -0.0378 0.0181  357 ASN B OD1 
5685 N ND2 . ASN B 356 ? 0.5579 0.5038 0.3979 0.0471  -0.0215 0.0195  357 ASN B ND2 
5686 N N   . ALA B 357 ? 0.5298 0.4703 0.3407 0.0409  -0.0230 -0.0109 358 ALA B N   
5687 C CA  . ALA B 357 ? 0.5389 0.4694 0.3307 0.0403  -0.0207 -0.0186 358 ALA B CA  
5688 C C   . ALA B 357 ? 0.6024 0.5445 0.4024 0.0385  -0.0353 -0.0301 358 ALA B C   
5689 O O   . ALA B 357 ? 0.6187 0.5516 0.3991 0.0383  -0.0370 -0.0380 358 ALA B O   
5690 C CB  . ALA B 357 ? 0.5293 0.4575 0.3324 0.0354  -0.0025 -0.0177 358 ALA B CB  
5691 N N   . ILE B 358 ? 0.5457 0.5064 0.3740 0.0369  -0.0450 -0.0319 359 ILE B N   
5692 C CA  . ILE B 358 ? 0.6086 0.5811 0.4498 0.0347  -0.0576 -0.0433 359 ILE B CA  
5693 C C   . ILE B 358 ? 0.6087 0.5807 0.4348 0.0407  -0.0763 -0.0464 359 ILE B C   
5694 O O   . ILE B 358 ? 0.6550 0.6297 0.4836 0.0452  -0.0824 -0.0396 359 ILE B O   
5695 C CB  . ILE B 358 ? 0.5514 0.5423 0.4310 0.0300  -0.0570 -0.0442 359 ILE B CB  
5696 C CG1 . ILE B 358 ? 0.5159 0.5069 0.4090 0.0248  -0.0410 -0.0421 359 ILE B CG1 
5697 C CG2 . ILE B 358 ? 0.5895 0.5924 0.4850 0.0280  -0.0696 -0.0558 359 ILE B CG2 
5698 C CD1 . ILE B 358 ? 0.4607 0.4652 0.3854 0.0209  -0.0388 -0.0405 359 ILE B CD1 
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